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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
6PRQ
Type
protein
Length
161 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P00634, Q56237

Structure

solution nmr · 1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein161—P00634, Q56237

Compared structures

  • 6PRQ · 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 0.72

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