Research workbench

Structural Basis for Client Recognition and Activity of Hsp40 Chaperones

Analyse Structural Basis for Client Recognition and Activity of Hsp40 Chaperones in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6PQE
Type: protein
Length: 89 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: NOT
Source: Escherichia coli (strain K12); Thermus thermophilus (strain HB8 / ATCC 27634 /…
Molecule: Alkaline phosphatase,Chaperone protein DnaJ 2 fusion
EC: 3.1.3.1
UniProt: P00634, Q56237

Structure

solution nmr · resolution NOT · 1 distinct chain · 7% helix, 45% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Alkaline phosphatase,Chaperone protein DnaJ 2 fusion (EC 3.1.3.1)	protein	89	7% helix, 45% strand	P00634, Q56237

Compared structures

6PQE · Structural basis for client recognition and activity of HSP40 chaperones · the same entry in another collection · chain A against A, TM-score 1.00
Q56237 · AlphaFold monomer V2.0 prediction for chaperone protein dnaj 2 (Q56237) · a predicted model of the same protein · chain A against A, TM-score 0.64
P00634 · AlphaFold monomer V2.0 prediction for alkaline phosphatase (P00634) · a predicted model of the same protein · chain A against A, TM-score 0.36

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 P00634
Every structure of UniProt Q56237
Elsewhere: RCSB PDB 6PQE · PDBe 6PQE · UniProt P00634 · UniProt Q56237

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