1kay

X-ray diffraction
1.7Å resolution

70KD HEAT SHOCK COGNATE PROTEIN ATPASE DOMAIN, K71A MUTANT

Released:
Source organism: Bos taurus
Primary publication:
Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis.
J. Biol. Chem. 271 15874-8 (1996)
PMID: 8663302

Function and Biology Details

Reaction catalysed:
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock cognate 71 kDa protein Chain: A
Molecule details ›
Chain: A
Length: 381 amino acids
Theoretical weight: 41.94 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P19120 (Residues: 1-381; Coverage: 59%)
Gene names: HSC70, HSPA8
Structure domains:

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 143.9Å b: 64.6Å c: 46.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.243
Expression system: Not provided