Research workbench
Vim-2, a zn-beta-lactamase from pseudomonas aeruginosa with an oxidized cys (cysteinesulfonic)
Analyse Vim-2, a zn-beta-lactamase from pseudomonas aeruginosa with an oxidized cys… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1KO2
- Type
- protein
- Length
- 230 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vim-2 metallo-beta-lactamase
- EC
- 3.5.2.6
- UniProt
- Q9K2N0
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.43
Structure
x-ray diffraction · 1 distinct chain · 26% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vim-2 metallo-beta-lactamase (EC 3.5.2.6) | protein | 230 | 26% helix, 30% strand | Q9K2N0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 134 | 0.43 | 0.76 | 18 | empty |
Modifications
Observed in the structure: 1 modified (oxidation).
Compared structures
- 1KO2 · VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with an oxidized Cys… · 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 1KO2 · PDBe 1KO2 · UniProt Q9K2N0
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