Phosphorus in PDB 1ake: Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State

Enzymatic activity of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State

All present enzymatic activity of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State:
2.7.4.3;

Protein crystallography data

The structure of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State, PDB code: 1ake was solved by C.W.Mueller, G.E.Schulz, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 10.00 / 2.00
Space group P 21 2 21
Cell size a, b, c (Å), α, β, γ (°) 73.200, 79.800, 85.000, 90.00, 90.00, 90.00
R / Rfree (%) 19.6 / n/a

Phosphorus Binding Sites:

Pages:

>>> Page 1 <<< Page 2, Binding sites: 11 - 11;

Binding sites:

The binding sites of Phosphorus atom in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State (pdb code 1ake). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 11 binding sites of Phosphorus where determined in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State, PDB code: 1ake:
Jump to Phosphorus binding site number: 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;

Phosphorus binding site 1 out of 11 in 1ake

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Phosphorus binding site 1 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P215

b:17.8
occ:1.00
 PA A:AP5215 0.0 17.8 1.0
O2A A:AP5215 1.4 15.2 1.0
O1A A:AP5215 1.5 16.5 1.0
O5F A:AP5215 1.6 19.7 1.0
O3A A:AP5215 1.6 19.1 1.0
C5F A:AP5215 2.6 15.1 1.0
PB A:AP5215 2.9 16.6 1.0
O2B A:AP5215 3.1 17.2 1.0
O3B A:AP5215 3.6 16.0 1.0
CA A:GLY12 3.7 20.6 1.0
C4F A:AP5215 3.8 20.8 1.0
OG1 A:THR15 3.8 17.7 1.0
O A:HOH320 3.8 19.8 1.0
O1B A:AP5215 3.9 15.2 1.0
N A:GLY12 3.9 15.8 1.0
C3F A:AP5215 4.0 14.5 1.0
NH1 A:ARG123 4.0 23.2 1.0
C A:GLY12 4.1 19.3 1.0
C2F A:AP5215 4.2 15.1 1.0
N A:LYS13 4.2 15.7 1.0
N A:GLY14 4.2 17.7 1.0
N A:THR15 4.2 17.7 1.0
C8A A:AP5215 4.5 15.5 1.0
CG2 A:VAL132 4.5 24.2 1.0
O4F A:AP5215 4.5 17.3 1.0
CA A:GLY10 4.6 18.4 1.0
CG1 A:VAL132 4.6 27.9 1.0
CA A:GLY14 4.7 17.9 1.0
C1F A:AP5215 4.7 12.6 1.0
CB A:THR15 4.7 15.4 1.0
C A:GLY10 4.8 19.4 1.0
O A:GLY12 4.8 19.0 1.0
C A:GLY14 4.9 22.9 1.0
CD A:ARG123 4.9 19.1 1.0
PG A:AP5215 5.0 19.7 1.0

Phosphorus binding site 2 out of 11 in 1ake

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Phosphorus binding site 2 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P215

b:16.6
occ:1.00
 PB A:AP5215 0.0 16.6 1.0
O2B A:AP5215 1.4 17.2 1.0
O1B A:AP5215 1.5 15.2 1.0
O3A A:AP5215 1.6 19.1 1.0
O3B A:AP5215 1.6 16.0 1.0
PG A:AP5215 2.9 19.7 1.0
PA A:AP5215 2.9 17.8 1.0
O2G A:AP5215 3.1 30.1 1.0
N A:LYS13 3.4 15.7 1.0
O2A A:AP5215 3.5 15.2 1.0
O1G A:AP5215 3.5 22.4 0.5
O3G A:AP5215 3.5 22.4 0.5
O1A A:AP5215 3.6 16.5 1.0
NZ A:LYS13 3.8 14.1 1.0
N A:GLY12 3.8 15.8 1.0
N A:GLY14 3.8 17.7 1.0
N A:GLY10 3.9 21.9 1.0
O5F A:AP5215 3.9 19.7 1.0
CA A:GLY10 3.9 18.4 1.0
O A:HOH362 4.0 22.3 1.0
N A:ALA11 4.0 16.8 1.0
CB A:LYS13 4.0 14.4 1.0
O1G A:AP5215 4.1 18.2 0.5
O3G A:AP5215 4.1 18.2 0.5
CA A:LYS13 4.2 14.6 1.0
O A:HOH320 4.2 19.8 1.0
C A:GLY12 4.2 19.3 1.0
C A:GLY10 4.2 19.4 1.0
NH1 A:ARG123 4.3 23.2 1.0
CA A:GLY12 4.3 20.6 1.0
C5F A:AP5215 4.5 15.1 1.0
CE A:LYS13 4.5 16.8 1.0
C A:LYS13 4.5 23.5 1.0
CG A:LYS13 4.8 16.1 1.0
CA A:GLY14 4.8 17.9 1.0
C A:ALA11 4.8 18.0 1.0
CA A:ALA11 5.0 18.3 1.0
O A:HOH429 5.0 30.7 1.0

Phosphorus binding site 3 out of 11 in 1ake

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Phosphorus binding site 3 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P215

b:19.7
occ:1.00
 PG A:AP5215 0.0 19.7 1.0
O2G A:AP5215 1.5 30.1 1.0
O1G A:AP5215 1.5 22.4 0.5
O3G A:AP5215 1.5 22.4 0.5
O1G A:AP5215 1.6 18.2 0.5
O3G A:AP5215 1.6 18.2 0.5
O3B A:AP5215 1.6 16.0 1.0
PD A:AP5215 2.8 32.1 0.5
PD A:AP5215 2.9 37.0 0.5
PB A:AP5215 2.9 16.6 1.0
O3D A:AP5215 2.9 34.5 0.5
O1E A:AP5215 2.9 34.5 0.5
O2D A:AP5215 3.2 43.6 0.5
O2B A:AP5215 3.3 17.2 1.0
O A:HOH355 3.6 55.7 1.0
NH1 A:ARG123 3.6 23.2 1.0
O2D A:AP5215 3.6 32.8 0.5
O1B A:AP5215 3.6 15.2 1.0
O1D A:AP5215 3.8 25.4 0.5
O A:HOH429 3.8 30.7 1.0
N A:GLY10 3.8 21.9 1.0
O1D A:AP5215 3.9 43.6 0.5
O A:HOH362 4.0 22.3 1.0
PE A:AP5215 4.0 25.8 1.0
O3A A:AP5215 4.1 19.1 1.0
NH2 A:ARG167 4.2 18.4 0.5
NH1 A:ARG167 4.2 27.9 0.5
NZ A:LYS13 4.2 14.1 1.0
O3D A:AP5215 4.3 36.1 0.5
O1E A:AP5215 4.3 36.1 0.5
O A:HOH320 4.3 19.8 1.0
CA A:PRO9 4.5 17.5 1.0
NH2 A:ARG123 4.5 17.6 1.0
CZ A:ARG123 4.6 20.7 1.0
O2E A:AP5215 4.6 31.6 1.0
CA A:GLY10 4.6 18.4 1.0
C A:PRO9 4.7 21.2 1.0
CZ A:ARG167 4.7 23.0 0.5
O A:HOH316 4.7 29.8 1.0
O2A A:AP5215 4.8 15.2 1.0
CE A:LYS13 4.9 16.8 1.0
NH1 A:ARG156 4.9 18.9 1.0
PA A:AP5215 5.0 17.8 1.0

Phosphorus binding site 4 out of 11 in 1ake

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Phosphorus binding site 4 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 4 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P215

b:37.0
occ:0.50
 PD A:AP5215 0.0 37.0 0.5
O2D A:AP5215 1.5 43.6 0.5
O1D A:AP5215 1.5 43.6 0.5
O1G A:AP5215 1.6 22.4 0.5
O3G A:AP5215 1.6 22.4 0.5
O3D A:AP5215 2.1 36.1 0.5
O1E A:AP5215 2.1 36.1 0.5
NH1 A:ARG156 2.4 18.9 1.0
PE A:AP5215 2.8 25.8 1.0
PG A:AP5215 2.9 19.7 1.0
O3D A:AP5215 2.9 34.5 0.5
O1E A:AP5215 2.9 34.5 0.5
O2D A:AP5215 3.0 32.8 0.5
O A:HOH316 3.0 29.8 1.0
PD A:AP5215 3.1 32.1 0.5
NH2 A:ARG156 3.2 21.2 1.0
CZ A:ARG156 3.3 22.4 1.0
O1G A:AP5215 3.3 18.2 0.5
O3G A:AP5215 3.3 18.2 0.5
NH1 A:ARG123 3.7 23.2 1.0
O A:HOH320 3.8 19.8 1.0
O2G A:AP5215 3.8 30.1 1.0
O2E A:AP5215 3.8 31.6 1.0
O A:HOH341 3.9 36.6 1.0
NH2 A:ARG123 3.9 17.6 1.0
NH1 A:ARG36 4.0 20.0 1.0
O3B A:AP5215 4.1 16.0 1.0
NH2 A:ARG36 4.1 15.4 1.0
O5J A:AP5215 4.1 27.0 1.0
CZ A:ARG123 4.1 20.7 1.0
NH2 A:ARG167 4.3 18.4 0.5
O A:HOH362 4.3 22.3 1.0
C5J A:AP5215 4.4 17.1 1.0
CZ A:ARG36 4.5 14.1 1.0
NE A:ARG156 4.5 23.9 1.0
O1D A:AP5215 4.6 25.4 0.5
O A:HOH429 4.6 30.7 1.0
NH1 A:ARG167 4.8 27.9 0.5
CZ A:ARG167 4.9 23.0 0.5
O2B A:AP5215 4.9 17.2 1.0

Phosphorus binding site 5 out of 11 in 1ake

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Phosphorus binding site 5 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 5 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P215

b:32.1
occ:0.50
 PD A:AP5215 0.0 32.1 0.5
O2D A:AP5215 1.5 32.8 0.5
O1D A:AP5215 1.5 25.4 0.5
O1G A:AP5215 1.6 18.2 0.5
O3G A:AP5215 1.6 18.2 0.5
O3D A:AP5215 1.6 34.5 0.5
O1E A:AP5215 1.6 34.5 0.5
NH1 A:ARG167 1.7 27.9 0.5
CZ A:ARG167 2.1 23.0 0.5
NH2 A:ARG167 2.2 18.4 0.5
O2D A:AP5215 2.6 43.6 0.5
PG A:AP5215 2.8 19.7 1.0
PE A:AP5215 3.0 25.8 1.0
PD A:AP5215 3.1 37.0 0.5
O1G A:AP5215 3.2 22.4 0.5
O3G A:AP5215 3.2 22.4 0.5
O2G A:AP5215 3.3 30.1 1.0
NE A:ARG167 3.4 24.6 0.5
NE A:ARG167 3.6 23.3 0.5
O A:HOH355 3.6 55.7 1.0
O5J A:AP5215 3.7 27.0 1.0
O3D A:AP5215 3.8 36.1 0.5
O1E A:AP5215 3.8 36.1 0.5
C5J A:AP5215 3.9 17.1 1.0
NH2 A:ARG156 4.0 21.2 1.0
O A:HOH401 4.0 72.6 1.0
O3B A:AP5215 4.1 16.0 1.0
O A:HOH456 4.1 59.2 1.0
O2E A:AP5215 4.2 31.6 1.0
CB A:PRO9 4.2 19.0 1.0
CD A:ARG167 4.2 24.5 0.5
NH2 A:ARG88 4.2 22.3 1.0
CZ A:ARG167 4.2 16.8 0.5
CD A:ARG167 4.3 23.2 0.5
NH2 A:ARG167 4.3 5.5 0.5
NH2 A:ARG123 4.3 17.6 1.0
CA A:PRO9 4.3 17.5 1.0
O1D A:AP5215 4.6 43.6 0.5
NH1 A:ARG156 4.8 18.9 1.0
O A:HOH429 4.8 30.7 1.0
NH1 A:ARG123 4.8 23.2 1.0
N A:GLY10 4.9 21.9 1.0
CZ A:ARG156 4.9 22.4 1.0

Phosphorus binding site 6 out of 11 in 1ake

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Phosphorus binding site 6 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 6 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P215

b:25.8
occ:1.00
 PE A:AP5215 0.0 25.8 1.0
O3D A:AP5215 1.5 36.1 0.5
O1E A:AP5215 1.5 36.1 0.5
O2E A:AP5215 1.5 31.6 1.0
O5J A:AP5215 1.6 27.0 1.0
O3D A:AP5215 1.6 34.5 0.5
O1E A:AP5215 1.6 34.5 0.5
C5J A:AP5215 2.7 17.1 1.0
PD A:AP5215 2.8 37.0 0.5
PD A:AP5215 3.0 32.1 0.5
O2D A:AP5215 3.4 43.6 0.5
O1G A:AP5215 3.5 22.4 0.5
O3G A:AP5215 3.5 22.4 0.5
NH2 A:ARG88 3.5 22.3 1.0
O2D A:AP5215 3.5 32.8 0.5
O A:HOH429 3.6 30.7 1.0
O A:HOH316 3.8 29.8 1.0
O1D A:AP5215 3.9 43.6 0.5
C4J A:AP5215 3.9 20.8 1.0
O1D A:AP5215 3.9 25.4 0.5
NH1 A:ARG88 3.9 21.5 1.0
O2G A:AP5215 4.0 30.1 1.0
PG A:AP5215 4.0 19.7 1.0
O A:HOH307 4.1 21.2 1.0
O1G A:AP5215 4.1 18.2 0.5
O3G A:AP5215 4.1 18.2 0.5
NH1 A:ARG167 4.1 27.9 0.5
O4J A:AP5215 4.1 21.8 1.0
CZ A:ARG88 4.2 28.1 1.0
NH1 A:ARG36 4.3 20.0 1.0
NH2 A:ARG156 4.3 21.2 1.0
C8B A:AP5215 4.4 14.1 1.0
CA A:GLY32 4.4 21.9 1.0
O A:HOH355 4.4 55.7 1.0
C3J A:AP5215 4.5 18.2 1.0
CZ A:ARG167 4.6 23.0 0.5
NH1 A:ARG156 4.7 18.9 1.0
O A:HOH456 4.8 59.2 1.0
NH2 A:ARG167 4.9 18.4 0.5
N A:GLY32 4.9 16.3 1.0
CZ A:ARG156 4.9 22.4 1.0
C1J A:AP5215 4.9 14.8 1.0
NH2 A:ARG36 4.9 15.4 1.0
O A:HOH362 5.0 22.3 1.0

Phosphorus binding site 7 out of 11 in 1ake

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Phosphorus binding site 7 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 7 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P215

b:37.3
occ:1.00
 PA B:AP5215 0.0 37.3 1.0
O2A B:AP5215 1.5 33.3 1.0
O1A B:AP5215 1.5 32.1 1.0
O5F B:AP5215 1.6 31.8 1.0
O3A B:AP5215 1.6 30.6 1.0
C5F B:AP5215 2.6 30.6 1.0
PB B:AP5215 2.9 31.3 1.0
O2B B:AP5215 3.3 44.9 1.0
O3B B:AP5215 3.7 43.6 1.0
C4F B:AP5215 3.7 35.1 1.0
O B:HOH620 3.8 43.7 1.0
OG1 B:THR15 3.8 38.1 1.0
O1B B:AP5215 3.9 33.5 1.0
NH1 B:ARG123 3.9 33.3 1.0
CA B:GLY12 3.9 30.4 1.0
C3F B:AP5215 4.0 31.9 1.0
N B:GLY12 4.1 33.4 1.0
C2F B:AP5215 4.1 36.3 1.0
C B:GLY12 4.2 31.4 1.0
N B:LYS13 4.3 29.0 1.0
N B:THR15 4.4 37.4 1.0
N B:GLY14 4.5 30.0 1.0
C1F B:AP5215 4.5 38.3 1.0
C8A B:AP5215 4.5 29.9 1.0
O4F B:AP5215 4.5 39.0 1.0
CA B:GLY10 4.6 32.6 1.0
CG2 B:VAL132 4.6 44.9 1.0
CG1 B:VAL132 4.6 43.5 1.0
CB B:THR15 4.7 36.3 1.0
C B:GLY10 4.7 30.4 1.0
O B:GLY12 4.7 40.0 1.0
CD B:ARG123 4.7 34.2 1.0
O B:GLY10 4.9 34.4 1.0
N9A B:AP5215 5.0 34.9 1.0

Phosphorus binding site 8 out of 11 in 1ake

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Phosphorus binding site 8 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 8 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P215

b:31.3
occ:1.00
 PB B:AP5215 0.0 31.3 1.0
O1B B:AP5215 1.5 33.5 1.0
O2B B:AP5215 1.5 44.9 1.0
O3A B:AP5215 1.6 30.6 1.0
O3B B:AP5215 1.6 43.6 1.0
PG B:AP5215 2.9 45.7 1.0
PA B:AP5215 2.9 37.3 1.0
O2G B:AP5215 3.3 55.5 1.0
N B:LYS13 3.5 29.0 1.0
O2A B:AP5215 3.5 33.3 1.0
O1A B:AP5215 3.6 32.1 1.0
O1G B:AP5215 3.6 43.7 1.0
N B:GLY12 3.8 33.4 1.0
N B:GLY10 3.8 38.6 1.0
NZ B:LYS13 3.9 33.4 1.0
CA B:GLY10 4.0 32.6 1.0
O3G B:AP5215 4.0 58.1 1.0
N B:GLY14 4.0 30.0 1.0
N B:ALA11 4.1 34.0 1.0
CB B:LYS13 4.1 34.6 1.0
O5F B:AP5215 4.1 31.8 1.0
O B:HOH620 4.1 43.7 1.0
C B:GLY10 4.2 30.4 1.0
C B:GLY12 4.2 31.4 1.0
CA B:LYS13 4.2 35.0 1.0
NH1 B:ARG123 4.2 33.3 1.0
CE B:LYS13 4.3 40.4 1.0
CA B:GLY12 4.4 30.4 1.0
C5F B:AP5215 4.6 30.6 1.0
C B:LYS13 4.6 33.9 1.0
CG B:LYS13 4.7 41.1 1.0
C B:ALA11 4.8 35.8 1.0
CA B:ALA11 4.9 33.0 1.0
O B:ALA8 4.9 33.5 1.0

Phosphorus binding site 9 out of 11 in 1ake

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Phosphorus binding site 9 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 9 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P215

b:45.7
occ:1.00
 PG B:AP5215 0.0 45.7 1.0
O1G B:AP5215 1.5 43.7 1.0
O2G B:AP5215 1.5 55.5 1.0
O3G B:AP5215 1.6 58.1 1.0
O3B B:AP5215 1.6 43.6 1.0
PB B:AP5215 2.9 31.3 1.0
PD B:AP5215 3.0 63.5 1.0
O2B B:AP5215 3.3 44.9 1.0
O3D B:AP5215 3.4 62.9 1.0
O B:HOH655 3.6 42.8 1.0
NH1 B:ARG123 3.7 33.3 1.0
PE B:AP5215 3.7 54.6 1.0
O1B B:AP5215 3.7 33.5 1.0
O2D B:AP5215 3.8 60.3 1.0
O1E B:AP5215 3.9 72.0 1.0
O1D B:AP5215 3.9 49.0 1.0
O2E B:AP5215 4.0 43.2 1.0
O B:HOH620 4.0 43.7 1.0
O3A B:AP5215 4.1 30.6 1.0
N B:GLY10 4.2 38.6 1.0
NZ B:LYS13 4.3 33.4 1.0
NH1 B:ARG156 4.6 43.6 1.0
CZ B:ARG123 4.7 36.9 1.0
CE B:LYS13 4.7 40.4 1.0
NH2 B:ARG123 4.7 40.2 1.0
O2A B:AP5215 4.8 33.3 1.0
CA B:PRO9 4.8 29.1 1.0
O B:HOH616 5.0 43.7 1.0

Phosphorus binding site 10 out of 11 in 1ake

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Phosphorus binding site 10 out of 11 in the Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 10 of Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 Angstroms Resolution: A Model For A Catalytic Transition State within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P215

b:63.5
occ:1.00
 PD B:AP5215 0.0 63.5 1.0
O2D B:AP5215 1.5 60.3 1.0
O1D B:AP5215 1.5 49.0 1.0
O3D B:AP5215 1.6 62.9 1.0
O3G B:AP5215 1.6 58.1 1.0
PG B:AP5215 3.0 45.7 1.0
PE B:AP5215 3.0 54.6 1.0
NE B:ARG167 3.4 45.0 1.0
O1G B:AP5215 3.5 43.7 1.0
O1E B:AP5215 3.6 72.0 1.0
O2G B:AP5215 3.6 55.5 1.0
NH2 B:ARG156 3.9 37.9 1.0
O5J B:AP5215 3.9 56.4 1.0
O B:HOH655 4.0 42.8 1.0
CD B:ARG167 4.0 41.7 1.0
CZ B:ARG167 4.0 50.8 1.0
O3B B:AP5215 4.0 43.6 1.0
O2E B:AP5215 4.1 43.2 1.0
NH2 B:ARG167 4.1 49.6 1.0
NH2 B:ARG123 4.1 40.2 1.0
C5J B:AP5215 4.1 45.4 1.0
NH2 B:ARG88 4.2 51.6 1.0
CB B:PRO9 4.3 33.9 1.0
CA B:PRO9 4.3 29.1 1.0
NH1 B:ARG156 4.6 43.6 1.0
NH1 B:ARG123 4.7 33.3 1.0
CZ B:ARG156 4.8 38.6 1.0
CG B:PRO9 4.8 30.9 1.0
O B:HOH685 4.9 53.1 1.0
CZ B:ARG123 4.9 36.9 1.0
CD1 B:ILE120 4.9 57.7 1.0
N B:GLY10 4.9 38.6 1.0

Reference:

C.W.Muller, G.E.Schulz. Structure of the Complex Between Adenylate Kinase From Escherichia Coli and the Inhibitor AP5A Refined at 1.9 A Resolution. A Model For A Catalytic Transition State. J.Mol.Biol. V. 224 159 1992.
ISSN: ISSN 0022-2836
PubMed: 1548697
DOI: 10.1016/0022-2836(92)90582-5
Page generated: Fri Sep 25 13:04:39 2020

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