MolNFT v1 · #63462 · protein
The di zinc carbapenemase cpha N220G mutant
3FAI · Beta-lactamase: “The di zinc carbapenemase cpha N220G mutant”. X-ray diffraction, 3 ligands (ZN, CL, SO4), 1 pocket (best druggability 0.60). MolNFT v1 #63462 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3FAI
- Type
- protein
- Length
- 227 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase
- EC
- 3.5.2.6
- UniProt
- P26918
- Ligands
- ZN, CL, SO4
- Pockets
- 1 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 30% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase (EC 3.5.2.6) | protein | 227 | 30% helix, 26% strand | P26918 |
Ligands and binding sites
- ZN · Zinc ion · metal · 3 copies · chains A
- CL · Chloride ion · ion · 7 copies · chains A
- SO4 · Sulfate ion · ion · 7 copies · chains A
- GOL · Glycerol · additive · 3 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.60 | 0.82 | 21 | SO4 |
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 P26918
- Elsewhere: RCSB PDB 3FAI · PDBe 3FAI · UniProt P26918
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