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Metallo-Beta-Lactamase VIM-2 in complex with 1-benzyl-1H-imidazole-2-carboxylic acid

Analyse Metallo-Beta-Lactamase VIM-2 in complex with 1-benzyl-1H-imidazole-2-carboxylic… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7CHV
Type: protein
Length: 231 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.174
Source: Pseudomonas aeruginosa
Molecule: Beta-lactamase class B VIM-2
UniProt: Q9K2N0
Ligands: FZX, ZN
Pockets: 1 · best druggability 0.50

Structure

x-ray diffraction · resolution 2.174 · 1 distinct chain · 28% helix, 29% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase class B VIM-2	protein	231	28% helix, 29% strand	Q9K2N0

Ligands and binding sites

FZX · 1-(phenylmethyl)imidazole-2-carboxylic acid · ligand · chains A
ZN · Zinc ion · metal · 3 copies · chains A
FMT · Formic acid · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	194	0.50	0.77	24	ZN, FZX

Compared structures

7CHV · Metallo-beta-lactamase vim-2 in complex with 1-benzyl-1H-imidazole-2- carboxylic acid · 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 7CHV · PDBe 7CHV · UniProt Q9K2N0

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