3R4T
Crystal structure of 4-aminobutyrate aminotransferase GabT from Mycobacterium marinum covalently bound to pyridoxal phosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006526 | biological_process | L-arginine biosynthetic process |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0019752 | biological_process | carboxylic acid metabolic process |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0047298 | molecular_function | (S)-3-amino-2-methylpropionate transaminase activity |
| A | 0047589 | molecular_function | 5-aminovalerate transaminase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MPD A 446 |
| Chain | Residue |
| A | SER172 |
| A | ASN222 |
| A | ALA311 |
| A | HIS313 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 447 |
| Chain | Residue |
| A | MET94 |
| A | TYR153 |
| A | ARG156 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 448 |
| Chain | Residue |
| A | LEU10 |
| site_id | AC4 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL A 450 |
| Chain | Residue |
| A | ARG352 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 451 |
| Chain | Residue |
| A | ALA27 |
| A | HOH471 |
| A | HOH537 |
| A | HOH653 |
| A | HOH654 |
Functional Information from PROSITE/UniProt
| site_id | PS00600 |
| Number of Residues | 38 |
| Details | AA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FIaDEVqt.GFaRtGamfacdhenvep....DLIvtAKgiaDG |
| Chain | Residue | Details |
| A | PHE259-GLY296 |
