Research workbench
Crystal structure of the oxacillin-hydrolyzing class D extended- spectrum beta-lactamase oxa-14 from pseudomonas aeruginosa
Analyse Crystal structure of the oxacillin-hydrolyzing class D extended- spectrum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7L5R
- Type
- protein
- Length
- 483 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase
- EC
- 3.5.2.6
- UniProt
- Q59648
- Ligands
- SO4
- Pockets
- 4 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase (EC 3.5.2.6) | protein | 247 | 39% helix, 22% strand | Q59648 |
| B | Beta-lactamase (EC 3.5.2.6) | protein | 236 | 37% helix, 24% strand | Q59648 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 145 | 0.71 | 0.90 | 29 | empty |
| 2 | 170 | 0.49 | 0.77 | 35 | SO4 |
| 3 | 134 | 0.41 | 0.75 | 28 | SO4 |
| 4 | 56 | 0.35 | 0.78 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1312 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide, 1 modified (disulfide, carboxylation).
Compared structures
- 7L5R · Crystal Structure of the Oxacillin-hydrolyzing Class D Extended-spectrum Beta-lactamase… · 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 Q59648
- Elsewhere: RCSB PDB 7L5R · PDBe 7L5R · UniProt Q59648
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