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Structure of yeast oxysterol binding protein OSH4 in complex with 7-hydroxycholesterol

Analyse Structure of yeast oxysterol binding protein OSH4 in complex with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1ZHT
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: HCR
Pockets: 11 · best druggability 0.85

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	KES1 protein	protein	436	32% helix, 28% strand	P35844

Ligands and binding sites

HCR · 7-hydroxycholesterol · ligand · chains A

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

Pockets

11 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	528	0.85	0.91	53	HCR
2	128	0.51	0.80	20	empty
3	85	0.46	0.81	26	empty
4	88	0.46	0.80	21	empty
5	162	0.45	0.75	21	empty

Compared structures

1ZHT · Structure of yeast oxysterol binding protein Osh4 in complex with 7-hydroxycholesterol · 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 1ZHT · PDBe 1ZHT · UniProt P35844

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