MolNFT v1 · #101564 · protein

C212A mutant of synechococcus vkor

4NV6 · VKORC1/THIOREDOXIN domain protein: “C212A mutant of synechococcus vkor”. X-ray diffraction, 1 ligand (U10), 3 pockets (best druggability 0.77). MolNFT v1 #101564 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4NV6
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: VKORC1/THIOREDOXIN domain protein
UniProt: Q2JJF6
Ligands: U10
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 59% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VKORC1/THIOREDOXIN domain protein	protein	264	59% helix, 7% strand	Q2JJF6

Ligands and binding sites

U10 · Ubiquinone-10 · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	259	0.77	0.89	37	U10
2	180	0.49	0.76	29	empty
3	53	0.38	0.80	11	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

4NV6 · C212A mutant of Synechococcus VKOR · the same entry in another collection · chain A against A, TM-score 1.00
Q2JJF6 · AlphaFold monomer V2.0 prediction for vitamin K epoxide reductase homolog (Q2JJF6) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 Q2JJF6
Elsewhere: RCSB PDB 4NV6 · PDBe 4NV6 · UniProt Q2JJF6

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