› 5hph

X-ray diffraction
2.43Å resolution

Structure of TRAP1 fragment

Released:
DOI: 10.2210/pdb5hph/pdb
PDB entry 5hph coloured by chain, front view.
PDB entry 5hph coloured by chain, side view.
PDB entry 5hph coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
2.4 Å resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrix.
Sung N, Lee J, Kim JH, Chang C, Tsai FT, Lee S
Acta Crystallogr D Struct Biol 72 904-11 (2016)
PMID: 27487821

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: 500 amino acids
Theoretical weight: 56.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12931 (Residues: 60-554; Coverage: 70%)
Gene names: HSP75, HSPC5, TRAP1
Sequence domains: Hsp90 protein

Ligands and Environments

5 bound ligands:
Ligand ANP 2 x ANP
Ligand PO4 3 x PO4
Ligand MG 2 x MG
Ligand GOL 4 x GOL
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 93.437Å b: 104.946Å c: 156.909Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.195 0.238
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Hsp90 and Hsp70 chaperones: Collaborators in protein remodeling.
Genest et al. (2019)
1 more

1 mention without citation

2.4 Å resolution crystal structure of human TRAP1NM, the Hsp90 paralog in the mitochondrial matrix.
Sung et al. (2016)