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 | 0016829 | molecular_function | lyase activity |
| A | 0016831 | molecular_function | carboxy-lyase activity |
| A | 0019481 | biological_process | L-alanine catabolic process, by transamination |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0047432 | molecular_function | 2,2-dialkylglycine decarboxylase (pyruvate) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 435 |
| Chain | Residue |
| A | ALA95 |
| A | THR98 |
| A | PRO99 |
| A | LEU102 |
| A | HOH540 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 437 |
| Chain | Residue |
| A | THR110 |
| A | GLY111 |
| A | ALA112 |
| A | ASN115 |
| A | TRP138 |
| A | HIS139 |
| A | GLU210 |
| A | ASP243 |
| A | ALA245 |
| A | GLN246 |
| A | LYS272 |
| A | THR302 |
| A | THR303 |
| A | MES434 |
| A | HOH555 |
| A | HOH557 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MES A 434 |
| Chain | Residue |
| A | GLN52 |
| A | TRP138 |
| A | ALA152 |
| A | SER215 |
| A | GLN246 |
| A | LYS272 |
| A | ARG406 |
| A | PLP437 |
| site_id | ACT |
| Number of Residues | 22 |
| Details | ACTIVE SITE: THE COFACTOR PLP IS COVALENTLY BOUND |
| Chain | Residue |
| A | GLN52 |
| A | GLU210 |
| A | SER214 |
| A | SER215 |
| A | ASP243 |
| A | ALA245 |
| A | GLN246 |
| A | LYS272 |
| A | PLP437 |
| A | TYR301 |
| A | THR303 |
| A | MET53 |
| A | ASN394 |
| A | ARG406 |
| A | MES434 |
| A | PHE79 |
| A | THR110 |
| A | GLY111 |
| A | ASN115 |
| A | SER137 |
| A | TRP138 |
| A | MET141 |
| site_id | ME1 |
| Number of Residues | 5 |
| Details | METAL BINDING SITE 1 (NEAR THE ACTIVE SITE): LIGANDS TO THE LI+ ION ARE INDICATED |
| Chain | Residue |
| A | LEU78 |
| A | ASP307 |
| A | HOH539 |
| A | HOH552 |
| A | LI436 |
| site_id | ME2 |
| Number of Residues | 6 |
| Details | METAL BINDING SITE 2: LIGANDS TO THE NA+ ION ARE INDICATED |
| Chain | Residue |
| A | ALA95 |
| A | THR98 |
| A | PRO99 |
| A | LEU102 |
| A | HOH540 |
| A | NA435 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LIlDEAqt.GVgRtGtmfacqrdgvtp....DILtlSKtlgAG |
| Chain | Residue | Details |
| A | LEU240-GLY277 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine |
| Chain | Residue | Details |
| A | THR273 | |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 482 |
| Chain | Residue | Details |
| A | HIS139 | steric role |
| A | PRO211 | steric role, transition state stabiliser |
| A | GLU244 | electrostatic stabiliser, increase electrophilicity |
| A | THR247 | electrostatic stabiliser |
| A | THR273 | covalent catalysis, proton shuttle (general acid/base) |
| A | ILE407 | steric role, transition state stabiliser |
