MolNFT v1 · #169730 · protein

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

6XLF: “Full-length HSC82 in complex with AHA1 in the presence of AMP-pnp”. Electron microscopy, 3 ligands (ANP, MG, K). MolNFT v1 #169730 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6XLF
Type: protein
Length: 1,680 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt: P15108, Q12449
Ligands: ANP, MG, K

Structure

electron microscopy · 4 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	609	—	P15108
B	—	protein	610	—	P15108
C	—	protein	316	—	Q12449
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

6XLF · Full-length Hsc82 in complex with Aha1 in the presence of AMP-PNP · the same entry in another collection · chain D against D, 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 B 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 D 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 6XLF · PDBe 6XLF · UniProt P15108 · UniProt Q12449

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.