Research workbench
Metallo-beta-lactamase in complex with L-159,061
Analyse Metallo-beta-lactamase in complex with L-159,061 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A8T
- Type
- protein
- Length
- 458 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Metallo-beta-lactamase
- EC
- 3.5.2.6
- UniProt
- P25910
- Ligands
- 061, ZN
- Pockets
- 2 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Metallo-beta-lactamase (EC 3.5.2.6) | protein | 230 | 23% helix, 30% strand | P25910 |
| B | Metallo-beta-lactamase (EC 3.5.2.6) | protein | 228 | 24% helix, 31% strand | P25910 |
Ligands and binding sites
- 061 · 2-butyl-6-hydroxy-3-[2'-(1H-tetrazol-5-yl)-biphenyl-4-ylmethyl]-3H-quinazolin-4-one · ligand · chains A
- ZN · Zinc ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 197 | 0.53 | 0.78 | 24 | ZN |
| 2 | 155 | 0.51 | 0.79 | 21 | 061 |
Interfaces
1 interface between chains.
- A–B · 485 Ų buried · 12 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 1A8T · PDBe 1A8T · UniProt P25910
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