MolNFT v1 · #166280 · protein

Structure of human ketohexokinase-C in complex with fructose, NO3, and osthole

6UL7: “Structure of human ketohexokinase-C in complex with fructose, NO3, and osthole”. X-ray diffraction, 3 ligands (A0O, FRU, NO3), 1 pocket (best druggability 0.72). MolNFT v1 #166280 on GenesisL1: 3D structure, binding sites and…

PDB: 6UL7
Type: protein
Length: 297 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ketohexokinase
EC: 2.7.1.3
UniProt: P50053
Ligands: A0O, FRU, NO3
Pockets: 1 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ketohexokinase (EC 2.7.1.3)	protein	297	36% helix, 25% strand	P50053

Ligands and binding sites

A0O · 7-methoxy-8-(3-methylbut-2-enyl)chromen-2-one · ligand · chains A
FRU · beta-D-fructofuranose · sugar · chains A
NO3 · Nitrate ion · ion · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	537	0.72	0.81	55	FRU, A0O, NO3

Compared structures

6UL7 · Structure of human ketohexokinase-C in complex with fructose, NO3, and osthole · the same entry in another collection · chain A against A, TM-score 1.00
P50053 · AlphaFold monomer V2.0 prediction for ketohexokinase (P50053) · 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 P50053
Elsewhere: RCSB PDB 6UL7 · PDBe 6UL7 · UniProt P50053

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