3OKS
Crystal structure of 4-aminobutyrate transaminase from mycobacterium smegmatis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008483 | molecular_function | transaminase activity |
| A | 0009448 | biological_process | gamma-aminobutyric 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 |
| B | 0008483 | molecular_function | transaminase activity |
| B | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| B | 0042802 | molecular_function | identical protein binding |
| C | 0008483 | molecular_function | transaminase activity |
| C | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| C | 0042802 | molecular_function | identical protein binding |
| D | 0008483 | molecular_function | transaminase activity |
| D | 0009448 | biological_process | gamma-aminobutyric acid metabolic process |
| D | 0030170 | molecular_function | pyridoxal phosphate binding |
| D | 0034386 | molecular_function | 4-aminobutyrate:2-oxoglutarate transaminase activity |
| D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 455 |
| Chain | Residue |
| A | ALA163 |
| A | LYS172 |
| A | ILE182 |
| A | ARG184 |
| A | HOH587 |
| A | HOH588 |
| C | TYR183 |
| C | HOH486 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 480 |
| Chain | Residue |
| A | HIS152 |
| A | FMT470 |
| A | HOH816 |
| C | GLN218 |
| A | ASP151 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT A 460 |
| Chain | Residue |
| A | TYR154 |
| A | ARG157 |
| A | HOH492 |
| A | HOH1264 |
| B | MET95 |
| B | GLY320 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 465 |
| Chain | Residue |
| A | ASP257 |
| A | ARG306 |
| A | ILE309 |
| A | HOH659 |
| A | HOH988 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT A 470 |
| Chain | Residue |
| A | ASP151 |
| A | HIS152 |
| A | TYR416 |
| A | EDO480 |
| A | HOH1503 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 455 |
| Chain | Residue |
| B | ALA163 |
| B | LYS172 |
| B | ILE182 |
| B | ARG184 |
| B | HOH494 |
| B | HOH496 |
| B | HOH505 |
| D | TYR183 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 480 |
| Chain | Residue |
| B | ASP151 |
| B | HIS152 |
| B | TYR416 |
| B | FMT470 |
| B | HOH1590 |
| D | GLN218 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT B 460 |
| Chain | Residue |
| A | MET95 |
| A | GLY320 |
| B | TYR154 |
| B | ARG157 |
| B | HOH530 |
| B | HOH1316 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE FMT B 465 |
| Chain | Residue |
| B | HIS141 |
| B | ASP257 |
| B | HOH700 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT B 470 |
| Chain | Residue |
| B | HIS152 |
| B | TYR416 |
| B | EDO480 |
| B | HOH1335 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FMT B 475 |
| Chain | Residue |
| A | GLU100 |
| A | HOH478 |
| B | ARG19 |
| B | VAL54 |
| B | HOH554 |
| B | HOH1573 |
| C | HIS10 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 448 |
| Chain | Residue |
| C | HOH459 |
| C | HOH564 |
| C | HOH1319 |
| C | HOH1352 |
| C | HOH1364 |
| C | HOH1442 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO C 455 |
| Chain | Residue |
| A | TYR183 |
| C | ALA163 |
| C | LYS172 |
| C | ILE182 |
| C | ARG184 |
| C | HOH487 |
| C | HOH638 |
| C | HOH1453 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO C 480 |
| Chain | Residue |
| A | GLN218 |
| C | ASP151 |
| C | HIS152 |
| C | HOH481 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT C 460 |
| Chain | Residue |
| C | TYR154 |
| C | ARG157 |
| C | HOH523 |
| C | HOH1275 |
| D | MET95 |
| D | GLY320 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FMT C 465 |
| Chain | Residue |
| C | HIS141 |
| C | ASP257 |
| C | ARG306 |
| C | HOH586 |
| C | HOH737 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO D 455 |
| Chain | Residue |
| D | HOH682 |
| B | TYR183 |
| D | ALA163 |
| D | LYS172 |
| D | ILE182 |
| D | ARG184 |
| D | HOH484 |
| D | HOH493 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO D 480 |
| Chain | Residue |
| B | GLN218 |
| D | ASP151 |
| D | HIS152 |
| D | TYR416 |
| D | FMT470 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO D 485 |
| Chain | Residue |
| D | THR38 |
| D | CYS400 |
| D | HIS404 |
| D | VAL410 |
| D | LEU411 |
| D | SER412 |
| D | HOH451 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FMT D 460 |
| Chain | Residue |
| C | MET95 |
| C | GLY320 |
| D | TYR154 |
| D | ARG157 |
| D | HOH944 |
| D | HOH1269 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT D 465 |
| Chain | Residue |
| D | HIS141 |
| D | ASP257 |
| D | ARG306 |
| D | HOH605 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FMT D 470 |
| Chain | Residue |
| D | ASP151 |
| D | HIS152 |
| D | TYR416 |
| D | EDO480 |
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.GFaRtGamfacehegidp....DLIvtAKgiaGG |
| Chain | Residue | Details |
| A | PHE260-GLY297 |
