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Crystal structure of the oxa-10 W154G mutant at pH 7.0
Analyse Crystal structure of the oxa-10 W154G mutant at pH 7.0 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HP5
- Type
- protein
- Length
- 948 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase pse-2
- EC
- 3.5.2.6
- UniProt
- P14489
- Ligands
- CO, SO4
- Pockets
- 14 · best druggability 0.74
Structure
x-ray diffraction · 4 distinct chains · 40% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase pse-2 (EC 3.5.2.6) | protein | 246 | 39% helix, 21% strand | P14489 |
| B | Beta-lactamase pse-2 (EC 3.5.2.6) | protein | 238 | 40% helix, 24% strand | P14489 |
| C | Beta-lactamase pse-2 (EC 3.5.2.6) | protein | 231 | 40% helix, 24% strand | P14489 |
| D | Beta-lactamase pse-2 (EC 3.5.2.6) | protein | 233 | 40% helix, 23% strand | P14489 |
Ligands and binding sites
- CO · Cobalt (II) ion · metal · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 10 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 177 | 0.74 | 0.91 | 34 | empty |
| 2 | 154 | 0.70 | 0.89 | 34 | empty |
| 3 | 188 | 0.69 | 0.87 | 35 | empty |
| 4 | 111 | 0.67 | 0.90 | 24 | empty |
| 5 | 214 | 0.56 | 0.79 | 43 | SO4 |
Interfaces
3 interfaces between chains.
- C–D · 1339 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 1263 Ų buried · 16 hydrogen bonds · protein-protein
- A–C · 305 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
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 2HP5 · PDBe 2HP5 · UniProt P14489
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