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Crystal structure of OSH1 ank domain from saccharomyces cerevisia

Analyse Crystal structure of OSH1 ank domain from saccharomyces cerevisia in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5H28
Type: protein
Length: 263 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oxysterol-binding protein homolog 1
UniProt: P35845
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 57% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oxysterol-binding protein homolog 1	protein	263	57% helix, 0% strand	P35845

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.47	0.81	21	empty

Compared structures

5H28 · Crystal structure of Osh1 ANK domain from Saccharomyces cerevisia · the same entry in another collection · chain A against A, TM-score 1.00
P35845 · AlphaFold monomer V2.0 prediction for oxysterol-binding protein homolog 1 (P35845) · 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 P35845
Elsewhere: RCSB PDB 5H28 · PDBe 5H28 · UniProt P35845

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