1atr

X-ray diffraction
2.34Å resolution

THREONINE 204 OF THE CHAPERONE PROTEIN HSC70 INFLUENCES THE STRUCTURE OF THE ACTIVE SITE BUT IS NOT ESSENTIAL FOR ATP HYDROLYSIS

Released:

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: 386 amino acids
Theoretical weight: 42.51 KDa
Source organism: Bos taurus
Expression system: Not provided
UniProt:
  • Canonical: P19120 (Residues: 1-386; Coverage: 59%)
Gene names: HSC70, HSPA8
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 145.3Å b: 65Å c: 46.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 not available
Expression system: Not provided