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S. cerevisiae HSP104:CASEIN complex, middle domain conformation

Analyse S. cerevisiae HSP104:CASEIN complex, middle domain conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5VY9
Type: protein
Length: 4,866 residues
Chains: 7
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P31539
Ligands: AGS

Structure

electron microscopy · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, E, F	—	protein	849	—	P31539
C, D	—	protein	721	—	P31539
P	—	protein	28	—	—

Ligands and binding sites

AGS · Phosphothiophosphoric acid-adenylate ester · ligand · 12 copies · chains A, F, B, C, D, E

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

5VY9 · S. cerevisiae Hsp104:casein complex, Middle Domain Conformation · the same entry in another collection · chain B against B, TM-score 1.00
P31539 · AlphaFold monomer V2.0 prediction for heat shock protein 104 (P31539) · a predicted model of the same protein · chain C against A, TM-score 0.89

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 P31539
Elsewhere: RCSB PDB 5VY9 · PDBe 5VY9 · UniProt P31539

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