› 3esk

X-ray diffraction
2.05Å resolution

Structure of HOP TPR2A domain in complex with the non-cognate Hsc70 peptide ligand

Released:
DOI: 10.2210/pdb3esk/pdb
PDB entry 3esk coloured by chain, front view.
PDB entry 3esk coloured by chain, side view.
PDB entry 3esk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Electrostatic interactions of Hsp-organizing protein tetratricopeptide domains with Hsp70 and Hsp90: computational analysis and protein engineering.
Kajander T, Sachs JN, Goldman A, Regan L
J Biol Chem 284 25364-74 (2009)
PMID: 19586912

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 domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145676 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Stress-induced-phosphoprotein 1 Chain: A
Molecule details ›
Chain: A
Length: 129 amino acids
Theoretical weight: 15.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31948 (Residues: 223-350; Coverage: 24%)
Gene name: STIP1
Sequence domains:
Structure domains: Tetratricopeptide repeat domain
Heat shock cognate 71 kDa protein Chain: B
Molecule details ›
Chain: B
Length: 12 amino acids
Theoretical weight: 1.16 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P11142 (Residues: 635-646; Coverage: 2%)
Gene names: HSC70, HSP73, HSPA10, HSPA8

Ligands and Environments

1 bound ligand:
Ligand NI 1 x NI
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: C2
Unit cell:
a: 73.459Å b: 48.023Å c: 37.896Å
α: 90° β: 91.56° γ: 90°
R-values:
R R work R free
0.183 0.177 0.244
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

13 review citations

HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting.
Stricher et al. (2013)
12 more

4 mentions without citation

Modulation of protein fate decision by small molecules: targeting molecular chaperone machinery.
Wang et al. (2020)
3 more