Human vkor C43S mutant with vitamin K1 epoxide

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 32% strand (DSSP).

Ligands and binding sites

• CRO · {2-[(1R,2R)-1-amino-2-hydroxypropyl]-4-(4-hydroxybenzylidene)-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · chains A
• UAV · (2R,3R)-2-hydroxy-3-methyl-2-[(2E,7S)-3,7,11,15-tetramethylhexadec-2-en-1-yl]-2,3-dihydronaphthalene-1,4-dione · ligand · chains A

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

Pockets

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

Modifications

Observed in the structure: 2 cofactor, 1 covalent, 1 disulfide (chromophore, covalent ligand, disulfide).

Compared structures

• 6WV5 · Human VKOR C43S mutant with vitamin K1 epoxide · the same entry in another collection · chain A against A, TM-score 1.00
• Q9BQB6 · AlphaFold monomer V2.0 prediction for vitamin K epoxide reductase complex subunit 1… · a predicted model of the same protein · chain A against A, TM-score 0.39

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 A0A059PIQ0
• Every structure of UniProt Q9BQB6
• Elsewhere: RCSB PDB 6WV5 · PDBe 6WV5 · UniProt A0A059PIQ0 · UniProt Q9BQB6