› 5e86

X-ray diffraction
2.68Å resolution

isolated SBD of BiP with loop34 modification

Released:
DOI: 10.2210/pdb5e86/pdb
PDB entry 5e86 coloured by chain, front view.
PDB entry 5e86 coloured by chain, side view.
PDB entry 5e86 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:
  • not assigned
Cellular component:
  • not assigned
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 Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 26.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P11021 (Residues: 418-637; Coverage: 34%)
Gene names: GRP78, HSPA5
Sequence domains: Hsp70 protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: C2221
Unit cell:
a: 34.536Å b: 82.593Å c: 150.776Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.216 0.256
Expression system: Escherichia coli BL21

Quick links

Citations

9 review citations

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

2 mentions without citation

Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP.
Yang et al. (2015)
1 more