› 5f1x

X-ray diffraction
1.9Å resolution

Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ATP

Released:
DOI: 10.2210/pdb5f1x/pdb
PDB entry 5f1x coloured by chain, front view.
PDB entry 5f1x coloured by chain, side view.
PDB entry 5f1x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Probing the ATP Site of GRP78 with Nucleotide Triphosphate Analogs.
Hughes SJ, Antoshchenko T, Chen Y, Lu H, Pizarro JC, Park HW
PLoS One 11 e0154862 (2016)
PMID: 27144892

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 400 amino acids
Theoretical weight: 44.36 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P11021 (Residues: 26-407; Coverage: 60%)
Gene names: GRP78, HSPA5
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ATP 2 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 55.965Å b: 74.823Å c: 90.222Å
α: 90° β: 98.85° γ: 90°
R-values:
R R work R free
0.183 0.181 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

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)
2 more

8 mentions without citation

GRP78: A cell's response to stress.
Ibrahim et al. (2019)
7 more