Research workbench
Vim-2_10B. metallo-beta-lactamase inhibitors by bioisosteric replacement: preparation, activity and binding
Analyse Vim-2_10B. metallo-beta-lactamase inhibitors by bioisosteric replacement… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5NHZ
- Type
- protein
- Length
- 460 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9K2N0
- Ligands
- 8XZ, ZN, MG, PO4, CL, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | — | protein | 230 | — | Q9K2N0 |
Ligands and binding sites
- 8XZ · [(2~{R})-1-ethanoylsulfanyl-5-phenyl-pentan-2-yl]phosphonic acid · ligand · 2 copies · chains A, B
- ZN · Zinc ion · metal · 5 copies · chains A, B
- MG · Magnesium ion · metal
- PO4 · Phosphate ion · ion · 3 copies · chains A, B
- CL · Chloride ion · ion · chains A
- SO4 · Sulfate ion · ion · chains B
- PEG · Di(hydroxyethyl)ether · additive · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5NHZ · VIM-2_10b. Metallo-beta-Lactamase Inhibitors by Bioisosteric Replacement: Preparation… · 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 Q9K2N0
- Elsewhere: RCSB PDB 5NHZ · PDBe 5NHZ · UniProt Q9K2N0
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