› 1elw

X-ray diffraction
1.6Å resolution

Crystal structure of the TPR1 domain of HOP in complex with a HSC70 peptide

Released:
DOI: 10.2210/pdb1elw/pdb
PDB entry 1elw coloured by chain, front view.
PDB entry 1elw coloured by chain, side view.
PDB entry 1elw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine.
Scheufler C, Brinker A, Bourenkov G, Pegoraro S, Moroder L, Bartunik H, Hartl FU, Moarefi I
Cell 101 199-210 (2000)
PMID: 10786835

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152176 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Stress-induced-phosphoprotein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 118 amino acids
Theoretical weight: 13.45 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P31948 (Residues: 1-118; Coverage: 22%)
Gene name: STIP1
Structure domains: Tetratricopeptide repeat domain
HSC70-PEPTIDE Chains: C, D
Molecule details ›
Chains: C, D
Length: 8 amino acids
Theoretical weight: 859 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
Ligand NI 4 x NI
Ligand TRS 4 x TRS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X12B
Spacegroup: P41
Unit cell:
a: 75.47Å b: 75.47Å c: 42.89Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 0.215
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

164 review citations

Molecular chaperones in protein folding and proteostasis.
Hartl et al. (2011)
163 more

45 mentions without citation

Features of protein-protein interactions that translate into potent inhibitors: topology, surface area and affinity.
Smith et al. (2012)
44 more