Research workbench
Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, trigonal crystal form
Analyse Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, trigonal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BC2
- Type
- protein
- Length
- 434 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallo beta-lactamase II
- EC
- 3.5.2.6
- UniProt
- P04190
- Ligands
- ZN, SO4
- Pockets
- 2 · best druggability 0.34
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metallo beta-lactamase II (EC 3.5.2.6) | protein | 218 | 27% helix, 32% strand | P04190 |
| B | Metallo beta-lactamase II (EC 3.5.2.6) | protein | 216 | 27% helix, 32% strand | P04190 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 83 | 0.34 | 0.75 | 21 | empty |
| 2 | 84 | 0.33 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 583 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 modified (oxidation).
Compared structures
- 2BC2 · Metallo beta-lactamase II from bacillus cereus 569/H/9 at pH 6.0, trigonal crystal form · 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 B against A, TM-score 0.99
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 2BC2 · PDBe 2BC2 · UniProt P04190
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