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JAC1 co-chaperone from saccharomyces cerevisiae

Analyse JAC1 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: 3UO2
Type: protein
Length: 310 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: J-type co-chaperone JAC1, mitochondrial
UniProt: P53193
Pockets: 2 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 71% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	J-type co-chaperone JAC1, mitochondrial	protein	160	74% helix, 0% strand	P53193
B	J-type co-chaperone JAC1, mitochondrial	protein	150	67% helix, 0% strand	P53193

Pockets

2 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	148	0.76	0.94	26	empty
2	139	0.36	0.72	19	empty

Interfaces

1 interface between chains.

A–B · 1230 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

3UO2 · Jac1 co-chaperone from Saccharomyces cerevisiae · the same entry in another collection · chain A against A, TM-score 1.00
P53193 · AlphaFold monomer V2.0 prediction for J-type co-chaperone JAC1, mitochondrial (P53193) · 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 P53193
Elsewhere: RCSB PDB 3UO2 · PDBe 3UO2 · UniProt P53193

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