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Mutagenesis of zinc ligand residue CYS221 reveals plasticity in the imp-1 metallo-B-lactamase active site

Analyse Mutagenesis of zinc ligand residue CYS221 reveals plasticity in the imp-1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4F6Z
Type: protein
Length: 221 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase
UniProt: Q79MP6
Ligands: ZN
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 32% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase	protein	221	26% helix, 32% strand	Q79MP6

Ligands and binding sites

ZN · Zinc ion · metal · chains A
FLC · Citrate anion · additive · 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	0.51	0.77	30	FLC

Compared structures

4F6Z · Mutagenesis of zinc ligand residue Cys221 reveals plasticity in the IMP-1… · 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 Q79MP6
Elsewhere: RCSB PDB 4F6Z · PDBe 4F6Z · UniProt Q79MP6

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