› 5e85

X-ray diffraction
2.57Å resolution

isolated SBD of BiP

Released:
DOI: 10.2210/pdb5e85/pdb
PDB entry 5e85 coloured by chain, front view.
PDB entry 5e85 coloured by chain, side view.
PDB entry 5e85 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: 236 amino acids
Theoretical weight: 26.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P11021 (Residues: 418-637; Coverage: 35%)
Gene names: GRP78, HSPA5
Sequence domains: Hsp70 protein

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: C2221
Unit cell:
a: 36.378Å b: 91.661Å c: 141.797Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.219 0.264
Expression system: Escherichia coli BL21

Quick links

Citations

8 review citations

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

15 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)
14 more