Research workbench
Metallo-beta-lactamase
Analyse 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
- 2BMI
- Type
- protein
- Length
- 458 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (class B beta-lactamase)
- EC
- 3.5.2.6
- UniProt
- P25910
- Ligands
- ZN, NA
- Pockets
- 4 · best druggability 0.40
Structure
x-ray diffraction · 2 distinct chains · 27% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (class B beta-lactamase) (EC 3.5.2.6) | protein | 228 | 27% helix, 34% strand | P25910 |
| B | Protein (class B beta-lactamase) (EC 3.5.2.6) | protein | 230 | 27% helix, 32% strand | P25910 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.40 | 0.75 | 22 | ZN |
| 2 | 100 | 0.39 | 0.76 | 22 | empty |
| 3 | 56 | 0.34 | 0.78 | 15 | empty |
| 4 | 68 | 0.33 | 0.75 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 587 Ų buried · 13 hydrogen bonds · protein-protein
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 P25910
- Elsewhere: RCSB PDB 2BMI · PDBe 2BMI · UniProt P25910
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