› 3ldo

X-ray diffraction
1.95Å resolution

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

Released:
DOI: 10.2210/pdb3ldo/pdb
PDB entry 3ldo coloured by chain, front view.
PDB entry 3ldo coloured by chain, side view.
PDB entry 3ldo coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Adenosine-derived inhibitors of 78 kDa glucose regulated protein (Grp78) ATPase: insights into isoform selectivity.
Macias AT, Williamson DS, Allen N, Borgognoni J, Clay A, Daniels Z, Dokurno P, Drysdale MJ, Francis GL, Graham CJ, Howes R, Matassova N, Murray JB, Parsons R, Shaw T, Surgenor AE, Terry L, Wang Y, Wood M, Massey AJ
J Med Chem 54 4034-41 (2011)
PMID: 21526763

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: 384 amino acids
Theoretical weight: 42.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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 ANP 2 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 55.615Å b: 74.563Å c: 89.952Å
α: 90° β: 98.54° γ: 90°
R-values:
R R work R free
0.206 0.202 0.256
Expression system: Escherichia coli

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Citations

16 review citations

HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.
Stricher et al. (2013)
15 more

2 mentions without citation

Oxidative stress-mediated aldehyde adduction of GRP78 in a mouse model of alcoholic liver disease: functional independence of ATPase activity and chaperone function.
Galligan et al. (2014)
1 more