Structure of kpc-2 bound to QPX7728 at 1.30 a

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 17% strand (DSSP).

Ligands and binding sites

• RM9 · (1aR,7bS)-5-fluoro-2-hydroxy-1,1a,2,7b-tetrahydrocyclopropa[c][1,2]benzoxaborinine-4-carboxylic acid · ligand · chains A
• QNA · (1~{A}~{R},7~{B}~{S})-5-fluoranyl-2,2-bis(oxidanyl)-1~{A},7~{B}-dihydro-1~{H}-cyclopropa[c][1, 2]benzoxaborinine-4-carboxylic acid · ligand · chains A
• SO4 · Sulfate ion · ion · 2 copies · chains A
• GOL · Glycerol · 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, 0 with a druggability of 0.5 or more.

Modifications

Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

• 6V1J · Structure of KPC-2 bound to QPX7728 at 1.30 A · the same entry in another collection · chain A against A, TM-score 1.00
• Q9F663 · AlphaFold monomer V2.0 prediction for carbapenem-hydrolyzing beta- lactamase kpc (Q9F663) · a predicted model of the same protein · 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 Q9F663
• Elsewhere: RCSB PDB 6V1J · PDBe 6V1J · UniProt Q9F663