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 |
