Research workbench
Crystal structure of the oxa-10 beta-lactamase from pseudomonas aeruginosa
Analyse Crystal structure of the oxa-10 beta-lactamase from pseudomonas aeruginosa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EWZ
- Type
- protein
- Length
- 971 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta lactamase oxa-10
- EC
- 3.5.2.6
- UniProt
- P14489
- Pockets
- 9 · best druggability 0.78
Structure
x-ray diffraction · 2 distinct chains · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Beta lactamase oxa-10 (EC 3.5.2.6) | protein | 243 | 40% helix, 22% strand | P14489 |
| D | Beta lactamase oxa-10 (EC 3.5.2.6) | protein | 242 | 40% helix, 23% strand | P14489 |
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 233 | 0.78 | 0.91 | 59 | empty |
| 2 | 71 | 0.72 | 0.97 | 22 | empty |
| 3 | 110 | 0.70 | 0.92 | 31 | empty |
| 4 | 129 | 0.52 | 0.81 | 22 | empty |
| 5 | 132 | 0.49 | 0.79 | 24 | empty |
Interfaces
2 interfaces between chains.
- B–D · 1329 Ų buried · 18 hydrogen bonds · protein-protein
- A–C · 1309 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 1EWZ · Crystal structure of the oxa-10 beta-lactamase from pseudomonas aeruginosa · the same entry in another collection · chain D against D, TM-score 1.00
- P14489 · AlphaFold monomer V2.0 prediction for beta-lactamase oxa-10 (P14489) · a predicted model of the same protein · chain B against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P14489
- Elsewhere: RCSB PDB 1EWZ · PDBe 1EWZ · UniProt P14489
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