Research workbench

Full-length HSC82 in complex with two AHA1 ctd in the presence of AMP- pnp

Analyse Full-length HSC82 in complex with two AHA1 ctd in the presence of AMP- pnp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6XLE
Type: protein
Length: 1,502 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P15108, Q12449
Ligands: ANP, MG, K

Structure

electron microscopy · 2 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	—	protein	606	—	P15108
C, D	—	protein	145	—	Q12449

Ligands and binding sites

ANP · Phosphoaminophosphonic acid-adenylate ester · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B
K · Potassium ion · metal · 2 copies · chains A, B

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

Compared structures

6XLE · Full-length Hsc82 in complex with two Aha1 CTD in the presence of AMP-PNP · the same entry in another collection · chain A against A, TM-score 1.00
P15108 · AlphaFold monomer V2.0 prediction for ATP-dependent molecular chaperone HSC82 (P15108) · a predicted model of the same protein · chain A against A, TM-score 0.97
Q12449 · AlphaFold monomer V2.0 prediction for HSP90 co-chaperone AHA1 (Q12449) · a predicted model of the same protein · chain C against A, TM-score 0.95

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 P15108
Every structure of UniProt Q12449
Elsewhere: RCSB PDB 6XLE · PDBe 6XLE · UniProt P15108 · UniProt Q12449

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