› 4j8f

X-ray diffraction
2.7Å resolution

Crystal structure of a fusion protein containing the NBD of Hsp70 and the middle domain of Hip

Released:
DOI: 10.2210/pdb4j8f/pdb
PDB entry 4j8f coloured by chain, front view.
PDB entry 4j8f coloured by chain, side view.
PDB entry 4j8f coloured by chain, top view.
Source organisms:
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:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143646 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock 70 kDa protein 1A; Hsc70-interacting protein Chain: A
Molecule details ›
Chain: A
Length: 561 amino acids
Theoretical weight: 62.42 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0DMV8 (Residues: 1-382; Coverage: 60%)
  • Canonical: P50503 (Residues: 77-247; Coverage: 47%)
Gene names: Fam10a1, HSP72, HSPA1, HSPA1A, HSX70, Hip, St13
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ADP 1 x ADP
Ligand MG 1 x MG
Ligand PO4 1 x PO4
Ligand IOD 17 x IOD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P41
Unit cell:
a: 65.596Å b: 65.596Å c: 141.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.194 0.261
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

16 review citations

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

5 mentions without citation

The remarkable multivalency of the Hsp70 chaperones.
Zuiderweg et al. (2017)
4 more