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Crystal structure of an HSP90-SBA1 closed chaperone complex

Analyse Crystal structure of an HSP90-SBA1 closed chaperone complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2CGE
Type
protein
Length
1,215 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ATP-dependent molecular chaperone HSP82
UniProt
P02829
Pockets
20 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, DATP-dependent molecular chaperone HSP82protein40544% helix, 15% strandP02829

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19220.790.8296empty
24680.710.8151empty
32150.570.7931empty
42070.560.7930empty
51880.550.7935empty

Interfaces

3 interfaces between chains.

  • A–D · 664 Ų buried · 6 hydrogen bonds · protein-protein
  • B–D · 636 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 610 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 2CGE · Crystal structure of an Hsp90-Sba1 closed chaperone complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P02829 · AlphaFold monomer V2.0 prediction for ATP-dependent molecular chaperone HSP82 (P02829) · a predicted model of the same protein · chain A against A, TM-score 0.91

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