› 4j8d

X-ray diffraction
2.8Å resolution

Middle domain of Hsc70-interacting protein, crystal form II

Released:
DOI: 10.2210/pdb4j8d/pdb
PDB entry 4j8d coloured by chain, front view.
PDB entry 4j8d coloured by chain, side view.
PDB entry 4j8d coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle.
Li Z, Hartl FU, Bracher A
Nat Struct Mol Biol 20 929-35 (2013)
PMID: 23812373

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156209 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Hsc70-interacting protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 175 amino acids
Theoretical weight: 19.76 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P50503 (Residues: 78-247; Coverage: 46%)
Gene names: Fam10a1, Hip, St13
Structure domains: Tetratricopeptide repeat domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 57.29Å b: 126.998Å c: 57.312Å
α: 90° β: 105.93° γ: 90°
R-values:
R R work R free
0.249 0.246 0.299
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

17 review citations

In vivo aspects of protein folding and quality control.
Balchin et al. (2016)
16 more

1 mention without citation

Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates.
Karunanayake et al. (2021)