3DXV
The crystal structure of alpha-amino-epsilon-caprolactam racemase from Achromobacter obae
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 | 0016853 | molecular_function | isomerase activity |
| A | 0019481 | biological_process | L-alanine catabolic process, by transamination |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0047463 | molecular_function | 2-aminohexano-6-lactam racemase activity |
| B | 0008453 | molecular_function | alanine-glyoxylate transaminase activity |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009436 | biological_process | glyoxylate catabolic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0019481 | biological_process | L-alanine catabolic process, by transamination |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0047463 | molecular_function | 2-aminohexano-6-lactam racemase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP A 450 |
| Chain | Residue |
| A | SER109 |
| A | HOH455 |
| A | HOH460 |
| B | GLN294 |
| B | THR295 |
| A | GLY110 |
| A | SER111 |
| A | TYR137 |
| A | HIS138 |
| A | GLU205 |
| A | ASP238 |
| A | LYS241 |
| A | LYS267 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE PLP B 450 |
| Chain | Residue |
| A | GLN294 |
| A | THR295 |
| A | HOH451 |
| B | SER109 |
| B | GLY110 |
| B | SER111 |
| B | TYR137 |
| B | HIS138 |
| B | GLU205 |
| B | SER209 |
| B | ASP238 |
| B | LYS241 |
| B | LYS267 |
| B | HOH456 |
| B | HOH462 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. VVcDEVkv.GLaRsGrlhcfehegfvp....DILvlGKglgGG |
| Chain | Residue | Details |
| A | VAL235-GLY272 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:19146406 |
| Chain | Residue | Details |
| A | TYR137 | |
| B | TYR137 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY110 | |
| B | GLY110 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | TYR137 | |
| A | ASP238 | |
| B | TYR137 | |
| B | ASP238 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19146406 |
| Chain | Residue | Details |
| A | THR295 | |
| B | THR295 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | LYS267 | |
| B | LYS267 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| A | ASP238 | |
| A | TYR137 | |
| A | LYS267 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| B | ASP238 | |
| B | TYR137 | |
| B | LYS267 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| A | ASP238 | |
| A | TYR137 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| B | ASP238 | |
| B | TYR137 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| A | ALA80 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1cl1 |
| Chain | Residue | Details |
| B | ALA80 |
