1GKF
Crystal structures of penicillin acylase enzyme-substrate complexes: Structural insights into the catalytic mechanism
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A (A) | PENICILLIN G ACYLASE ALPHA SUBUNIT | polymer | 260 | 28979.7 | 1 | UniProt (P06875) Pfam (PF01804) | ESCHERICHIA COLI | PENICILLIN AMIDOHYDROLASE, NTN, PENICILLIN G AMIDASE, PENICILLIN G AMIDOHYDROLASE |
| 2 | B (B) | PENICILLIN G ACYLASE BETA SUBUNIT | polymer | 557 | 62386.5 | 1 | UniProt (P06875) Pfam (PF01804) | ESCHERICHIA COLI | |
| 3 | C, D, E, F, G... (B) | 1,2-ETHANEDIOL | non-polymer | 62.1 | 13 | Chemie (EDO) | |||
| 4 | P (B) | CALCIUM ION | non-polymer | 40.1 | 1 | Chemie (CA) | |||
| 5 | Q, R (A, B) | water | water | 18.0 | 901 | Chemie (HOH) |
Sequence modifications
A: 1 - 260 (UniProt: P06875)
B: 1 - 557 (UniProt: P06875)
| PDB | External Database | Details |
|---|---|---|
| Sme 16 | Met 42 | modified residue |
| PDB | External Database | Details |
|---|---|---|
| Ala 241 | Asn 530 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 2 |
| Total formula weight | 91366.2 | |
| Non-Polymers* | Number of molecules | 14 |
| Total formula weight | 847.0 | |
| All* | Total formula weight | 92213.1 |
