Research workbench
Crystal structure of ctx-M-14 E166A/P167S/D240G beta-lactamase in complex with ceftazidime-2
Analyse Crystal structure of ctx-M-14 E166A/P167S/D240G beta-lactamase in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V8V
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase
- EC
- 3.5.2.6
- UniProt
- Q9L5C7
- Ligands
- CAZ
- Pockets
- 2 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase (EC 3.5.2.6) | protein | 260 | 42% helix, 20% strand | Q9L5C7 |
Ligands and binding sites
- CAZ · Acylated ceftazidime · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 218 | 0.64 | 0.83 | 41 | CAZ |
| 2 | 52 | 0.34 | 0.78 | 16 | empty |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 6V8V · Crystal structure of CTX-M-14 E166A/P167S/D240G beta-lactamase in complex with… · 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 Q9L5C7
- Elsewhere: RCSB PDB 6V8V · PDBe 6V8V · UniProt Q9L5C7
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