7VO1
Structure of aminotransferase-substrate complex
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0042802 | molecular_function | identical protein binding |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0042802 | molecular_function | identical protein binding |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIdDEVqm.GMgRtGrmwaiehfdivp....DIVtvAKalgGG |
| Chain | Residue | Details |
| A | LEU261-GLY298 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"35337912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7VNO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7VNT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Plays critical role in maintaining high affinity for the substrate","evidences":[{"source":"PubMed","id":"35337912","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"35337912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7VNT","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
