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Crystal structure of yeast HSP70 (BIP/KAR2) complexed with ADP

Analyse Crystal structure of yeast HSP70 (BIP/KAR2) complexed with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3QFU
Type
protein
Length
379 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
78 kda glucose-regulated protein homolog
UniProt
P16474
Ligands
ADP, MG, PO4
Pockets
3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A78 kda glucose-regulated protein homologprotein37941% helix, 28% strandP16474

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • PO4 · Phosphate ion · ion · 2 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12450.770.9137ADP, PO4, MG
24660.640.7747empty
3720.430.8114PO4

Compared structures

  • 3QFU · Crystal structure of Yeast Hsp70 (Bip/kar2) complexed with ADP · the same entry in another collection · chain A against A, TM-score 1.00
  • P16474 · AlphaFold monomer V2.0 prediction for endoplasmic reticulum chaperone bip (P16474) · a predicted model of the same protein · chain A against A, TM-score 0.91

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