Phosphorus in PDB 1a0g: L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate

Enzymatic activity of L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate

All present enzymatic activity of L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate:
2.6.1.21;

Protein crystallography data

The structure of L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate, PDB code: 1a0g was solved by S.Sugio, A.Kashima, K.Kishimoto, D.Peisach, G.A.Petsko, D.Ringe, T.Yoshimura, N.Esaki, with X-Ray Crystallography technique. A brief refinement statistics is given in the table below:

Resolution Low / High (Å) 50.00 / 2.00
Space group P 21 21 21
Cell size a, b, c (Å), α, β, γ (°) 77.340, 91.760, 88.690, 90.00, 90.00, 90.00
R / Rfree (%) 21.6 / 26.3

Phosphorus Binding Sites:

The binding sites of Phosphorus atom in the L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate (pdb code 1a0g). This binding sites where shown within 5.0 Angstroms radius around Phosphorus atom.
In total 2 binding sites of Phosphorus where determined in the L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate, PDB code: 1a0g:
Jump to Phosphorus binding site number: 1; 2;

Phosphorus binding site 1 out of 2 in 1a0g

Go back to Phosphorus Binding Sites List in 1a0g
Phosphorus binding site 1 out of 2 in the L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 1 of L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
A:P285

b:20.4
occ:1.00
P A:PMP285 0.0 20.4 1.0
O1P A:PMP285 1.5 20.2 1.0
O3P A:PMP285 1.5 22.2 1.0
O2P A:PMP285 1.5 23.8 1.0
O4P A:PMP285 1.6 26.2 1.0
C5A A:PMP285 2.6 32.2 1.0
OG1 A:THR241 3.5 21.5 1.0
O A:HOH322 3.6 21.3 1.0
N A:THR241 3.7 21.0 1.0
O A:HOH344 3.7 24.7 1.0
C5 A:PMP285 3.8 37.5 1.0
N A:ILE204 3.9 16.3 1.0
OG1 A:THR205 3.9 18.7 1.0
NH2 A:ARG50 4.1 17.8 1.0
CA A:GLY203 4.1 16.8 1.0
CA A:SER240 4.1 18.4 1.0
C4A A:PMP285 4.3 41.0 1.0
N A:THR205 4.3 15.9 1.0
C A:SER240 4.4 19.8 1.0
NH1 A:ARG50 4.4 18.4 1.0
CB A:THR241 4.4 20.5 1.0
C4 A:PMP285 4.5 39.8 1.0
C A:GLY203 4.5 17.3 1.0
CA A:THR241 4.6 21.4 1.0
CB A:THR205 4.7 16.2 1.0
C6 A:PMP285 4.7 38.0 1.0
CZ A:ARG50 4.7 19.4 1.0
CB A:SER240 4.7 18.3 1.0
CE1 A:HIS47 4.8 18.5 1.0
CA A:ILE204 4.8 16.9 1.0
CB A:ILE204 4.9 17.4 1.0
NZ A:LYS145 4.9 31.0 1.0

Phosphorus binding site 2 out of 2 in 1a0g

Go back to Phosphorus Binding Sites List in 1a0g
Phosphorus binding site 2 out of 2 in the L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate


Mono view


Stereo pair view

A full contact list of Phosphorus with other atoms in the P binding site number 2 of L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-Phosphate within 5.0Å range:
probe atom residue distance (Å) B Occ
B:P285

b:22.3
occ:1.00
P B:PMP285 0.0 22.3 1.0
O1P B:PMP285 1.4 23.2 1.0
O3P B:PMP285 1.5 24.8 1.0
O4P B:PMP285 1.6 29.1 1.0
O2P B:PMP285 1.6 23.2 1.0
C5A B:PMP285 2.5 32.2 1.0
O B:HOH302 3.6 21.7 1.0
OG1 B:THR241 3.7 17.5 1.0
N B:ILE204 3.8 21.5 1.0
C5 B:PMP285 3.8 36.0 1.0
O B:HOH340 3.8 16.2 1.0
N B:THR241 3.9 20.2 1.0
CA B:GLY203 3.9 21.3 1.0
OG1 B:THR205 4.0 18.7 1.0
NH2 B:ARG50 4.1 23.9 1.0
C4A B:PMP285 4.2 36.5 1.0
CA B:SER240 4.2 18.0 1.0
NH1 B:ARG50 4.2 23.2 1.0
C B:GLY203 4.3 21.2 1.0
N B:THR205 4.3 18.9 1.0
N4A B:PMP285 4.4 37.8 1.0
C4 B:PMP285 4.4 37.1 1.0
C B:SER240 4.5 19.9 1.0
CB B:THR241 4.5 19.1 1.0
CZ B:ARG50 4.7 23.6 1.0
CA B:THR241 4.7 20.6 1.0
C6 B:PMP285 4.7 36.1 1.0
CA B:ILE204 4.8 20.7 1.0
CB B:THR205 4.8 16.8 1.0
CB B:SER240 4.8 18.0 1.0
CB B:ILE204 4.9 20.9 1.0

Reference:

S.Sugio, A.Kashima, K.Kishimoto, D.Peisach, G.A.Petsko, D.Ringe, T.Yoshimura, N.Esaki. Crystal Structures of L201A Mutant of D-Amino Acid Aminotransferase at 2.0 A Resolution: Implication of the Structural Role of LEU201 in Transamination. Protein Eng. V. 11 613 1998.
ISSN: ISSN 0269-2139
PubMed: 9749913
DOI: 10.1093/PROTEIN/11.8.613
Page generated: Fri Sep 25 11:56:03 2020

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