6GIO
Structure of Amino Acid Amide Racemase from Ochrobactrum anthropi
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
A | 0008483 | molecular_function | transaminase activity |
A | 0009436 | biological_process | glyoxylate catabolic process |
A | 0019481 | biological_process | L-alanine catabolic process, by transamination |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
B | 0008483 | molecular_function | transaminase activity |
B | 0009436 | biological_process | glyoxylate catabolic process |
B | 0019481 | biological_process | L-alanine catabolic process, by transamination |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
C | 0008483 | molecular_function | transaminase activity |
C | 0009436 | biological_process | glyoxylate catabolic process |
C | 0019481 | biological_process | L-alanine catabolic process, by transamination |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
D | 0008483 | molecular_function | transaminase activity |
D | 0009436 | biological_process | glyoxylate catabolic process |
D | 0019481 | biological_process | L-alanine catabolic process, by transamination |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 14 |
Details | binding site for residue PLP D 501 |
Chain | Residue |
B | GLN294 |
D | VAL240 |
D | LYS241 |
D | LYS267 |
D | HOH611 |
D | HOH662 |
B | THR295 |
D | SER111 |
D | GLY112 |
D | SER113 |
D | TYR139 |
D | HIS140 |
D | GLU205 |
D | ASP238 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
B | GLY57 |
B | TYR58 |
B | GLY59 |
B | HIS60 |
B | ILE63 |
B | GLY271 |
D | VAL71 |
D | MET74 |
site_id | AC3 |
Number of Residues | 22 |
Details | binding site for Di-peptide PLP A 501 and LYS A 267 |
Chain | Residue |
A | ALA51 |
A | PRO53 |
A | SER111 |
A | GLY112 |
A | SER113 |
A | TYR139 |
A | HIS140 |
A | GLU205 |
A | ASP238 |
A | VAL240 |
A | LYS241 |
A | GLY266 |
A | GLY268 |
A | LEU269 |
A | GLY270 |
A | HOH623 |
A | HOH632 |
A | HOH634 |
A | HOH647 |
A | HOH653 |
C | GLN294 |
C | THR295 |
site_id | AC4 |
Number of Residues | 22 |
Details | binding site for Di-peptide PLP B 501 and LYS B 267 |
Chain | Residue |
B | ALA51 |
B | PRO53 |
B | SER111 |
B | GLY112 |
B | SER113 |
B | ASN116 |
B | TYR139 |
B | HIS140 |
B | GLU205 |
B | ASP238 |
B | VAL240 |
B | LYS241 |
B | GLY266 |
B | GLY268 |
B | LEU269 |
B | GLY270 |
B | HOH617 |
B | HOH625 |
B | HOH636 |
B | HOH694 |
D | GLN294 |
D | THR295 |
site_id | AC5 |
Number of Residues | 22 |
Details | binding site for Di-peptide PLP C 501 and LYS C 267 |
Chain | Residue |
A | GLN294 |
A | THR295 |
C | ALA51 |
C | PRO53 |
C | SER111 |
C | GLY112 |
C | SER113 |
C | TYR139 |
C | HIS140 |
C | GLU205 |
C | ASP238 |
C | VAL240 |
C | LYS241 |
C | GLY266 |
C | GLY268 |
C | LEU269 |
C | GLY270 |
C | HOH606 |
C | HOH611 |
C | HOH659 |
C | HOH663 |
C | HOH674 |
Functional Information from PROSITE/UniProt
site_id | PS00600 |
Number of Residues | 38 |
Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VVvDEVkv.GLgRtGlmhcfqheglep....DMVvfGKglgGG |
Chain | Residue | Details |
D | VAL235-GLY272 |