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Crystal structure of oxa-58 with disordered active site
Analyse Crystal structure of oxa-58 with disordered active site in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4Z9Q
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase oxa-58
- EC
- 3.5.2.6
- UniProt
- B2I3T3
- Pockets
- 2 · best druggability 0.47
Structure
x-ray diffraction · 1 distinct chain · 43% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase oxa-58 (EC 3.5.2.6) | protein | 224 | 43% helix, 21% strand | B2I3T3 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 164 | 0.47 | 0.76 | 24 | empty |
| 2 | 59 | 0.30 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 4Z9Q · Crystal structure of OXA-58 with disordered active site · the same entry in another collection · chain A 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 B2I3T3
- Elsewhere: RCSB PDB 4Z9Q · PDBe 4Z9Q · UniProt B2I3T3
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