Research workbench
Crystal structure of BLEG-1 B3 metallo-beta-lactamase
Analyse Crystal structure of BLEG-1 B3 metallo-beta-lactamase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7EV5
- Type
- protein
- Length
- 209 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.44
- Source
- Bacillus lehensis G1
- Molecule
- Lactamase_B domain-containing protein
- UniProt
- A0A060M4R1
- Ligands
- ZN, IOD
Structure
x-ray diffraction · resolution 1.44 · 1 distinct chain · 23% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Lactamase_B domain-containing protein | protein | 209 | 23% helix, 30% strand | A0A060M4R1 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 7EV5 · Crystal structure of bleg-1 B3 metallo-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 A0A060M4R1
- Elsewhere: RCSB PDB 7EV5 · PDBe 7EV5 · UniProt A0A060M4R1
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