MolNFT v1 · #112195 · protein
Structure of oxa-51 beta-lactamase
4ZDX: “Structure of oxa-51 beta-lactamase”. X-ray diffraction, 1 ligand (TOE), 1 pocket (best druggability 0.48). MolNFT v1 #112195 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4ZDX
- Type
- protein
- Length
- 241 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase
- UniProt
- Q5QT35
- Ligands
- TOE
- Pockets
- 1 · best druggability 0.48
Structure
x-ray diffraction · 1 distinct chain · 42% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase | protein | 241 | 42% helix, 21% strand | Q5QT35 |
Ligands and binding sites
- TOE · 2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxyl · ligand · chains A
- GOL · Glycerol · additive · 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 | 166 | 0.48 | 0.76 | 28 | TOE |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
- 4ZDX · Structure of OXA-51 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 Q5QT35
- Elsewhere: RCSB PDB 4ZDX · PDBe 4ZDX · UniProt Q5QT35
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