8PEC
OXA-48_Q5-CAZ. Epistasis Arises from Shifting the Rate-Limiting Step during Enzyme Evolution
Entity
| Entity ID | Chain ID | Description | Type | Chain length | Formula weight | Number of molecules | DB Name (Accession) | Biological source | Descriptive keywords |
| 1 | A, B, C, D (A, B, C, D) | Beta-lactamase | polymer | 242 | 28002.7 | 4 | UniProt (Q6XEC0) Pfam (PF00905) | Klebsiella pneumoniae | |
| 2 | E, G, I (A, C, D) | 1-({(2R)-2-[(1R)-1-{[(2Z)-2-(2-amino-1,3-thiazol-4-yl)-2-{[(2-carboxypropan-2-yl)oxy]imino}acetyl]amino}-2-oxoethyl]-4-carboxy-3,6-dihydro-2H-1,3-thiazin-5-yl}methyl)pyridinium | non-polymer | 549.6 | 3 | Chemie (CTJ) | |||
| 3 | F, H (A, C) | CHLORIDE ION | non-polymer | 35.5 | 2 | Chemie (CL) | |||
| 4 | J, K, L, M (A, B, C, D) | water | water | 18.0 | 84 | Chemie (HOH) |
Sequence modifications
A, B, C, D: 24 - 265 (UniProt: Q6XEC0)
| PDB | External Database | Details |
|---|---|---|
| Val 33 | Ala 33 | engineered mutation |
| Glu 51 | Lys 51 | engineered mutation |
| Leu 72 | Phe 72 | engineered mutation |
| Ala 212 | Ser 212 | engineered mutation |
| Ala 213 | Thr 213 | engineered mutation |
Sequence viewer
Contents of the asymmetric unit
| Polymers | Number of chains | 4 |
| Total formula weight | 112010.9 | |
| Non-Polymers* | Number of molecules | 5 |
| Total formula weight | 1719.7 | |
| All* | Total formula weight | 113730.6 |
