› 5evz

X-ray diffraction
1.85Å resolution

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

Released:
DOI: 10.2210/pdb5evz/pdb
PDB 5evz coloured by chain and viewed from the front.
PDB 5evz coloured by chain and viewed from the side.
PDB 5evz coloured by chain and viewed from the top.
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
OpenAccess logo 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)
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
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand MG 2 x MG
Ligand PO4 2 x PO4
Ligand ADP 2 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P21
Unit cell:
a: 55.55Å b: 74.802Å c: 89.22Å
α: 90° β: 98.6° γ: 90°
R-values:
R R work R free
0.167 0.165 0.205
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review 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)
5 other articles