› 5f3k

X-ray diffraction
1.82Å resolution

X-Ray Crystallographic Structure of hTrap1 N-terminal Domain-apo

Released:
DOI: 10.2210/pdb5f3k/pdb
PDB entry 5f3k coloured by chain, front view.
PDB entry 5f3k coloured by chain, side view.
PDB entry 5f3k coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Mitochondrial Hsp90 is a ligand-activated molecular chaperone coupling ATP binding to dimer closure through a coiled-coil intermediate.
Sung N, Lee J, Kim JH, Chang C, Joachimiak A, Lee S, Tsai FT
Proc Natl Acad Sci U S A 113 2952-7 (2016)
PMID: 26929380

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171445 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein 75 kDa, mitochondrial Chains: A, B
Molecule details ›
Chains: A, B
Length: 238 amino acids
Theoretical weight: 26.05 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12931 (Residues: 60-294; Coverage: 33%)
Gene names: HSP75, HSPC5, TRAP1
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P3221
Unit cell:
a: 65.25Å b: 65.25Å c: 233.372Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.183 0.182 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Structure, Function, and Regulation of the Hsp90 Machinery.
Biebl et al. (2019)
6 more

3 mentions without citation

Functional and Regulatory Roles of Fold-Switching Proteins.
Kim et al. (2021)
2 more