› 1yuw

X-ray diffraction
2.6Å resolution

crystal structure of bovine hsc70(aa1-554)E213A/D214A mutant

Released:
DOI: 10.2210/pdb1yuw/pdb
PDB entry 1yuw coloured by chain, front view.
PDB entry 1yuw coloured by chain, side view.
PDB entry 1yuw coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Structural basis of interdomain communication in the Hsc70 chaperone.
Jiang J, Prasad K, Lafer EM, Sousa R
Mol Cell 20 513-24 (2005)
PMID: 16307916

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-148503 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock cognate 71 kDa protein Chain: A
Molecule details ›
Chain: A
Length: 554 amino acids
Theoretical weight: 60.98 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P19120 (Residues: 1-554; Coverage: 85%)
Gene names: HSC70, HSPA8
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-D
Spacegroup: P21
Unit cell:
a: 65.694Å b: 50.14Å c: 87.156Å
α: 90° β: 99.86° γ: 90°
R-values:
R R work R free
0.22 0.22 0.297
Expression system: Escherichia coli

Quick links

Citations

35 review citations

Molecular chaperones and protein quality control.
Bukau et al. (2006)
34 more

45 mentions without citation

Mechanisms of the Hsp70 chaperone system.
Young JC. (2010)
44 more