Bacillus cereus metallo-beta-lactamase (bcii) arg (121) cys mutant. solved at PH4.5 using 20MM ZNSO4 in the buffer. 1MM dtt and 1MM tcep- hcl were used as reducing agents. CYS221 is reduced.

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 33% strand (DSSP).

Ligands and binding sites

• ZN · Zinc ion · metal · 4 copies · chains A, B
• SO4 · Sulfate ion · ion · 7 copies · chains A, B
• CL · Chloride ion · ion · chains B
• GOL · Glycerol · additive · 21 copies · chains A, B

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

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 556 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

• 2BG2 · Bacillus cereus metallo-beta-lactamase (BcII) Arg (121) Cys mutant. Solved at pH4.5 using… · the same entry in another collection · chain B against B, 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 B 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 2BG2 · PDBe 2BG2 · UniProt P04190