Phosphorus in PDB 1ai3: Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences

Enzymatic activity of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences

All present enzymatic activity of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences:
1.1.1.42;

Protein crystallography data

The structure of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences, PDB code: 1ai3 was solved by B.L.Stoddard, A.Mesecar, D.E.Koshland Junior, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 1.90
Space group P 43 21 2
Cell size a, b, c (Å), α, β, γ (°) 102.400, 102.400, 150.700, 90.00, 90.00, 90.00
R / Rfree (%) 18.8 / 22

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences (pdb code 1ai3). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 3 binding sites of Phosphorus where determined in the Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences, PDB code: 1ai3:
Jump to Phosphorus binding site number: 1; 2; 3;

Phosphorus binding site 1 out of 3 in 1ai3

Go back to Phosphorus Binding Sites List in 1ai3
Phosphorus binding site 1 out of 3 in the Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P417

b:45.2
occ:1.00
 PA A:NDO417 0.0 45.2 1.0
O2A A:NDO417 1.4 41.3 1.0
O3 A:NDO417 1.5 52.0 1.0
O5B A:NDO417 1.6 43.3 1.0
O1A A:NDO417 1.6 42.5 1.0
C5B A:NDO417 2.7 42.2 1.0
PN A:NDO417 2.9 45.6 1.0
O2N A:NDO417 3.5 54.8 1.0
O1N A:NDO417 3.7 52.8 1.0
C4B A:NDO417 3.9 37.1 1.0
O3B A:NDO417 4.0 35.9 1.0
O5D A:NDO417 4.2 41.2 1.0
C3B A:NDO417 4.2 45.5 1.0
CA A:GLY340 4.5 15.2 1.0
C5D A:NDO417 4.6 41.0 1.0
C3D A:NDO417 4.7 44.2 1.0

Phosphorus binding site 2 out of 3 in 1ai3

Go back to Phosphorus Binding Sites List in 1ai3
Phosphorus binding site 2 out of 3 in the Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P417

b:45.6
occ:1.00
 PN A:NDO417 0.0 45.6 1.0
O1N A:NDO417 1.5 52.8 1.0
O2N A:NDO417 1.5 54.8 1.0
O3 A:NDO417 1.6 52.0 1.0
O5D A:NDO417 1.8 41.2 1.0
C5D A:NDO417 2.8 41.0 1.0
PA A:NDO417 2.9 45.2 1.0
O5B A:NDO417 3.6 43.3 1.0
O1A A:NDO417 3.7 42.5 1.0
CD A:PRO343 3.8 15.6 1.0
O A:HOH518 3.8 44.6 1.0
C3D A:NDO417 3.9 44.2 1.0
C4D A:NDO417 3.9 39.5 1.0
O2A A:NDO417 4.0 41.3 1.0
CG A:PRO343 4.3 19.9 1.0
N A:ALA342 4.4 12.6 1.0
O3D A:NDO417 4.4 42.6 1.0
O3B A:NDO417 4.6 35.9 1.0
O4D A:NDO417 4.7 40.8 1.0
CA A:ALA342 4.7 13.3 1.0

Phosphorus binding site 3 out of 3 in 1ai3

Go back to Phosphorus Binding Sites List in 1ai3
Phosphorus binding site 3 out of 3 in the Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 3 of Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P417

b:49.7
occ:1.00
 P2B A:NDO417 0.0 49.7 1.0
O2X A:NDO417 1.5 48.6 1.0
O3X A:NDO417 1.5 51.0 1.0
O1X A:NDO417 1.5 44.2 1.0
O2B A:NDO417 1.6 38.1 1.0
C2B A:NDO417 2.7 40.8 1.0
NH2 A:ARG395 3.4 21.2 1.0
C1B A:NDO417 3.5 35.9 1.0
C3B A:NDO417 3.9 45.5 1.0
NH1 A:ARG395 4.1 21.2 1.0
CZ A:ARG395 4.2 21.2 1.0
O4B A:NDO417 4.3 41.2 1.0
O3B A:NDO417 4.3 35.9 1.0
C4B A:NDO417 4.4 37.1 1.0
N9A A:NDO417 4.7 43.4 1.0
N3A A:NDO417 4.8 47.6 1.0

Reference:

A.D.Mesecar, B.L.Stoddard, D.E.Koshland Jr.. Orbital Steering in the Catalytic Power of Enzymes: Small Structural Changes with Large Catalytic Consequences. Science V. 277 202 1997.
ISSN: ISSN 0036-8075
PubMed: 9211842
DOI: 10.1126/SCIENCE.277.5323.202
Page generated: Fri Sep 25 12:58:21 2020

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