› 5e84

X-ray diffraction
2.99Å resolution

ATP-bound state of BiP

Released:
DOI: 10.2210/pdb5e84/pdb
PDB entry 5e84 coloured by chain, front view.
PDB entry 5e84 coloured by chain, side view.
PDB entry 5e84 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP.
Yang J, Nune M, Zong Y, Zhou L, Liu Q
Structure 23 2191-2203 (2015)
PMID: 26655470

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145633 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endoplasmic reticulum chaperone BiP Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 606 amino acids
Theoretical weight: 67.21 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
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 ATP 6 x ATP
Ligand ZN 18 x ZN
Ligand MG 12 x MG
Ligand SO4 6 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P3221
Unit cell:
a: 222.468Å b: 222.468Å c: 209.46Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.245 0.243 0.287
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

ACE2: Evidence of role as entry receptor for SARS-CoV-2 and implications in comorbidities.
Zamorano Cuervo et al. (2020)
5 more

54 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)
53 more