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Metallo-beta-lactamase bcii CD substituted from bacillus cereus at 1.35 ångströms resolution

Analyse Metallo-beta-lactamase bcii CD substituted from bacillus cereus at 1.35… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1MQO
Type: protein
Length: 221 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-lactamase II
EC: 3.5.2.6
UniProt: P04190
Ligands: CD
Pockets: 1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 33% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-lactamase II (EC 3.5.2.6)	protein	221	26% helix, 33% strand	P04190

Ligands and binding sites

CD · Cadmium ion · metal · 3 copies · chains A
CIT · Citric acid · 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	140	0.51	0.80	23	CD, CIT

Compared structures

1MQO · Metallo-beta-lactamase BcII Cd substituted from Bacillus cereus at 1.35 angstroms… · the same entry in another collection · chain A against A, TM-score 1.00
P04190 · AlphaFold monomer V2.0 prediction for metallo-beta-lactamase type 2 (P04190) · a predicted model of the same protein · chain A against A, TM-score 0.99

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 P04190
Elsewhere: RCSB PDB 1MQO · PDBe 1MQO · UniProt P04190

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