MolNFT v1 · #29738 · protein

Structure of yeast oxysterol binding protein OSH4 in complex with cholesterol

1ZHY · KES1 protein: “Structure of yeast oxysterol binding protein OSH4 in complex with cholesterol”. X-ray diffraction, 2 ligands (CLR, PB), 10 pockets (best druggability 0.86). MolNFT v1 #29738 on GenesisL1: 3D structure, binding sites…

PDB: 1ZHY
Type: protein
Length: 436 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: KES1 protein
UniProt: P35844
Ligands: CLR, PB
Pockets: 10 · best druggability 0.86

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	KES1 protein	protein	436	31% helix, 28% strand	P35844

Ligands and binding sites

CLR · Cholesterol · ligand · chains A
PB · Lead (II) ion · metal · 2 copies · chains A

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

Pockets

10 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	539	0.86	0.91	64	CLR
2	109	0.48	0.80	16	empty
3	171	0.47	0.76	26	empty
4	100	0.47	0.80	27	empty
5	115	0.41	0.76	25	empty

Compared structures

1ZHY · Structure of yeast oxysterol binding protein Osh4 in complex with cholesterol · the same entry in another collection · chain A against A, TM-score 1.00
P35844 · AlphaFold monomer V2.0 prediction for oxysterol-binding protein homolog 4 (P35844) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P35844
Elsewhere: RCSB PDB 1ZHY · PDBe 1ZHY · UniProt P35844

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