2Q7W
Structural Studies Reveals the Inactivation of E. coli L-aspartate aminotransferase (S)-4,5-amino-dihydro-2-thiophenecarboxylic acid (SADTA) via two mechanisms at pH 6.0
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | Aspartate aminotransferase | polymer | 396 | 43744.3 | 1 | UniProt (P00509) Pfam (PF00155) | Escherichia coli | Transaminase A, ASPAT |
| 2 | B (A) | SULFATE ION | non-polymer | 96.1 | 1 | Chemie (SO4) | |||
| 3 | C (A) | 4-[({3-HYDROXY-2-METHYL-5-[(PHOSPHONOOXY)METHYL]PYRIDIN-4-YL}METHYL)AMINO]THIOPHENE-2-CARBOXYLIC ACID | non-polymer | 374.3 | 1 | Chemie (PSZ) | |||
| 4 | D (A) | 4'-DEOXY-4'-AMINOPYRIDOXAL-5'-PHOSPHATE | non-polymer | 248.2 | 1 | Chemie (PMP) | |||
| 5 | E, F, G, H, I... (A) | GLYCEROL | non-polymer | 92.1 | 11 | Chemie (GOL) | |||
| 6 | P (A) | water | water | 18.0 | 428 | Chemie (HOH) |
Sequence modifications
A: 1 - 396 (UniProt: P00509)
| PDB | External Database | Details |
|---|---|---|
| Kst 246 | Lys 246 | modified residue |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 1 |
| Total formula weight | 43744.3 | |
| Non-Polymers* | Number of molecules | 14 |
| Total formula weight | 1731.6 | |
| All* | Total formula weight | 45475.9 |
