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Phosphorus in PDB 1a0g: L201A Mutant of D-Amino Acid Aminotransferase Complexed with Pyridoxamine-5'-PhosphateEnzymatic 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:
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 1a0gGo 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
Phosphorus binding site 2 out of 2 in 1a0gGo 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
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.
Page generated: Fri Sep 25 11:56:03 2020
ISSN: ISSN 0269-2139 PubMed: 9749913 DOI: 10.1093/PROTEIN/11.8.613 |
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