MolNFT v1 · #101560 · protein

C50A mutant of synechococcus vkor, C2221 crystal form

4NV2 · VKORC1/THIOREDOXIN domain protein: “C50A mutant of synechococcus vkor, C2221 crystal form”. X-ray diffraction, 1 ligand (U10), 4 pockets (best druggability 0.78). MolNFT v1 #101560 on GenesisL1: 3D structure, binding sites and…

PDB: 4NV2
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: 4 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 58% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	VKORC1/THIOREDOXIN domain protein	protein	264	58% 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

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	284	0.78	0.89	38	U10
2	218	0.53	0.77	21	empty
3	63	0.44	0.81	11	empty
4	56	0.31	0.76	11	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

4NV2 · C50A mutant of Synechococcus VKOR, C2221 crystal form · 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 0.99

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 Q2JJF6
Elsewhere: RCSB PDB 4NV2 · PDBe 4NV2 · UniProt Q2JJF6

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