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Crystal structure of Hsp31

Analyse Crystal structure of Hsp31 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IZZ
Type: protein
Length: 276 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.31
Source: Escherichia coli
Molecule: Hsp31
UniProt: Q8XB78
Pockets: 1 · best druggability 0.55

Structure

x-ray diffraction · resolution 2.31 · 1 distinct chain · 37% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Hsp31	protein	276	37% helix, 17% strand	Q8XB78

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	64	0.55	0.87	19	empty

Compared structures

1IZZ · Crystal structure of HSP31 · the same entry in another collection · chain A against A, TM-score 1.00
Q8XB78 · AlphaFold monomer V2.0 prediction for PROTEIN/NUCLEIC acid deglycase hcha (Q8XB78) · a predicted model of the same protein · chain A against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q8XB78
Elsewhere: RCSB PDB 1IZZ · PDBe 1IZZ · UniProt Q8XB78

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