Research workbench

J-domain of SIS1 protein, HSP40 co-chaperone from saccharomyces cerevisiae

Analyse J-domain of SIS1 protein, HSP40 co-chaperone from saccharomyces cerevisiae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4RWU
Type: protein
Length: 81 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein SIS1
UniProt: P25294
Pockets: 1 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 62% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein SIS1	protein	81	62% helix, 0% strand	P25294

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	65	0.31	0.75	13	empty

Compared structures

4RWU · J-domain of Sis1 protein, Hsp40 co-chaperone from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
P25294 · AlphaFold monomer V2.0 prediction for protein SIS1 (P25294) · a predicted model of the same protein · chain A against A, TM-score 0.93

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 P25294
Elsewhere: RCSB PDB 4RWU · PDBe 4RWU · UniProt P25294

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.