MolNFT v1 · #168100 · protein
Class D beta-lactamase bsu-2
6W5E · Bsu-2 beta-lactamase: “Class D beta-lactamase bsu-2”. X-ray diffraction, 1 pocket (best druggability 0.42). MolNFT v1 #168100 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6W5E
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Bsu-2 beta-lactamase
- EC
- 3.5.2.6
- UniProt
- P54427
- Pockets
- 1 · best druggability 0.42
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Bsu-2 beta-lactamase (EC 3.5.2.6) | protein | 238 | 38% helix, 21% strand | P54427 |
Ligands and binding sites
- MLI · Malonate ion · additive · 3 copies · chains A
- EDO · 1,2-ethanediol · additive · 2 copies · 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 | 112 | 0.42 | 0.77 | 24 | MLI |
Modifications
Observed in the structure: 1 modified (carboxylation).
Compared structures
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 P54427
- Elsewhere: RCSB PDB 6W5E · PDBe 6W5E · UniProt P54427
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