Research workbench
Bacillus cereus zn-dependent metallo-beta-lactamase at pH 5.8
Analyse Bacillus cereus zn-dependent metallo-beta-lactamase at pH 5.8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3I13
- Type
- protein
- Length
- 214 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-lactamase 2
- EC
- 3.5.2.6
- UniProt
- P04190
- Ligands
- ZN
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-lactamase 2 (EC 3.5.2.6) | protein | 214 | 26% helix, 30% strand | P04190 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 3I13 · Bacillus cereus Zn-dependent metallo-beta-lactamase at pH 5.8 · the same entry in another collection · chain A against A, TM-score 1.00
- P04190 · AlphaFold monomer V2.0 prediction for metallo-beta-lactamase type 2 (P04190) · a predicted model of the same protein · 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 P04190
- Elsewhere: RCSB PDB 3I13 · PDBe 3I13 · UniProt P04190
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