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Chaperone complex

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

PDB
3CQX
Type
protein
Length
918 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P63017, Q91YN9

Structure

x-ray diffraction · 4 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein376—P63017
B—protein377—P63017
C—protein81—Q91YN9
D—protein84—Q91YN9

Compared structures

  • 3CQX · Chaperone Complex · the same entry in another collection · chain D against D, TM-score 1.00
  • Q91YN9 · AlphaFold monomer V2.0 prediction for bag family molecular chaperone regulator 2 (Q91YN9) · a predicted model of the same protein · chain C against A, TM-score 0.93
  • P63017 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P63017) · a predicted model of the same protein · chain B against A, TM-score 0.87

Analyse

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