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HSP90 co-chaperone CDC37

Analyse HSP90 co-chaperone CDC37 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2W0G
Type: protein
Length: 129 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HSP90 co-chaperone CDC37
UniProt: Q16543

Structure

x-ray diffraction · 1 distinct chain · 82% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HSP90 co-chaperone CDC37	protein	129	82% helix, 0% strand	Q16543

Compared structures

2W0G · HSP90 co-chaperone CDC37 · the same entry in another collection · chain A against A, TM-score 1.00
Q16543 · AlphaFold monomer V2.0 prediction for HSP90 co-chaperone CDC37 (Q16543) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 Q16543
Elsewhere: RCSB PDB 2W0G · PDBe 2W0G · UniProt Q16543

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