Research workbench

Human vkor with brodifacoum

Analyse Human vkor with brodifacoum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6WVH
Type: protein
Length: 768 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: A0A059PIQ0, Q9BQB6
Ligands: CRO, UA7

Structure

x-ray diffraction · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	380	—	A0A059PIQ0, Q9BQB6
B	—	protein	388	—	A0A059PIQ0, Q9BQB6

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 · 2 copies · chains A, B
UA7 · Brodifacoum · ligand · 2 copies · chains A, B
OLC · (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate · additive · 2 copies · chains A

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

Compared structures

6WVH · Human VKOR with Brodifacoum · 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 0.42

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 6WVH · PDBe 6WVH · UniProt A0A059PIQ0 · UniProt Q9BQB6

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