MolNFT v1 · #109521 · protein
Structure of the class D beta-lactamase oxa-160 V130D in acyl-enzyme complex with ceftazidime
4X56: “Structure of the class D beta-lactamase oxa-160 V130D in acyl-enzyme complex with ceftazidime”. X-ray diffraction, 1 ligand (CAZ), 1 pocket (best druggability 0.44). MolNFT v1 #109521 on GenesisL1: 3D structure, binding sites and…
- PDB
- 4X56
- Type
- protein
- Length
- 244 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Class D beta-lactamase oxa-160
- UniProt
- D2XKK9
- Ligands
- CAZ
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 1 distinct chain · 40% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Class D beta-lactamase oxa-160 | protein | 244 | 40% helix, 22% strand | D2XKK9 |
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
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 182 | 0.44 | 0.74 | 34 | CAZ |
Modifications
Observed in the structure: 1 covalent (covalent ligand).
Compared structures
- 4X56 · Structure of the class D Beta-Lactamase OXA-160 V130D in Acyl-Enzyme 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 D2XKK9
- Elsewhere: RCSB PDB 4X56 · PDBe 4X56 · UniProt D2XKK9
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