› 4cgw

X-ray diffraction
3Å resolution

Second TPR of Spaghetti (RPAP3) bound to HSP90 peptide SRMEEVD

Released:
DOI: 10.2210/pdb4cgw/pdb
PDB entry 4cgw coloured by chain, front view.
PDB entry 4cgw coloured by chain, side view.
PDB entry 4cgw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for phosphorylation-dependent recruitment of Tel2 to Hsp90 by Pih1.
Pal M, Morgan M, Phelps SE, Roe SM, Parry-Morris S, Downs JA, Polier S, Pearl LH, Prodromou C
Structure 22 805-18 (2014)
PMID: 24794838

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-139822 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RNA polymerase II-associated protein 3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 117 amino acids
Theoretical weight: 13.14 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H6T3 (Residues: 265-381; Coverage: 18%)
Gene name: RPAP3
Sequence domains: Tetratricopeptide repeat
Structure domains: Tetratricopeptide repeat domain
Heat shock protein HSP 90-alpha Chains: C, D
Molecule details ›
Chains: C, D
Length: 7 amino acids
Theoretical weight: 866 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P07900 (Residues: 726-732; Coverage: 1%)
Gene names: HSP90A, HSP90AA1, HSPC1, HSPCA

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P212121
Unit cell:
a: 63.57Å b: 96.51Å c: 52.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.244 0.241 0.291
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

13 review citations

Hsp90: breaking the symmetry.
Mayer et al. (2015)
12 more

3 mentions without citation

The Structure of the R2TP Complex Defines a Platform for Recruiting Diverse Client Proteins to the HSP90 Molecular Chaperone System.
Rivera-Calzada et al. (2017)
2 more