› 6asy

X-ray diffraction
1.85Å resolution

BiP-ATP2

Released:
DOI: 10.2210/pdb6asy/pdb
PDB entry 6asy coloured by chain, front view.
PDB entry 6asy coloured by chain, side view.
PDB entry 6asy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s.
Yang J, Zong Y, Su J, Li H, Zhu H, Columbus L, Zhou L, Liu Q
Nat Commun 8 1201 (2017)
PMID: 29084938

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmic reticulum chaperone BiP Chains: A, B
Molecule details ›
Chains: A, B
Length: 606 amino acids
Theoretical weight: 67.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P11021 (Residues: 25-633; Coverage: 95%)
Gene names: GRP78, HSPA5
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand GOL 8 x GOL
Ligand ATP 2 x ATP
Ligand SO4 8 x SO4
Ligand PO4 10 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P1
Unit cell:
a: 75.829Å b: 75.752Å c: 78.791Å
α: 62.05° β: 62.23° γ: 73.42°
R-values:
R R work R free
0.16 0.158 0.189
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

4 review citations

Structural and functional analysis of the Hsp70/Hsp40 chaperone system.
Liu et al. (2020)
3 more

10 mentions without citation

The endoplasmic reticulum (ER) chaperone BiP is a master regulator of ER functions: Getting by with a little help from ERdj friends.
Pobre et al. (2019)
9 more