4j8c

X-ray diffraction
1.1Å resolution

Crystal structure of the dimerization domain of Hsc70-interacting protein

Released:
Source organism: Rattus norvegicus
Primary publication:
Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle.
Nat Struct Mol Biol 20 929-35 (2013)
PMID: 23812373

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-156210 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hsc70-interacting protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 46 amino acids
Theoretical weight: 5.34 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P50503 (Residues: 1-44; Coverage: 12%)
Gene names: Fam10a1, Hip, St13
Sequence domains: Hsp70-interacting protein N N-terminal domain
Structure domains: Single alpha-helices involved in coiled-coils or other helix-helix interfaces

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 28.775Å b: 43.978Å c: 32.211Å
α: 90° β: 93.44° γ: 90°
R-values:
R R work R free
0.136 0.135 0.162
Expression system: Escherichia coli BL21(DE3)