› 5y3n

X-ray diffraction
2.4Å resolution

Structure of TRAP1 complexed with DN401

Released:
DOI: 10.2210/pdb5y3n/pdb
PDB entry 5y3n coloured by chain, front view.
PDB entry 5y3n coloured by chain, side view.
PDB entry 5y3n coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Paralog Specificity Determines Subcellular Distribution, Action Mechanism, and Anticancer Activity of TRAP1 Inhibitors.
Park HK, Jeong H, Ko E, Lee G, Lee JE, Lee SK, Lee AJ, Im JY, Hu S, Kim SH, Lee JH, Lee C, Kang S, Kang BH
J Med Chem 60 7569-7578 (2017)
PMID: 28816449

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-171444 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein 75 kDa, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 502 amino acids
Theoretical weight: 57.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli K-12
UniProt:
  • Canonical: Q12931 (Residues: 60-561; Coverage: 71%)
Gene names: HSP75, HSPC5, TRAP1
Sequence domains: Hsp90 protein

Ligands and Environments

1 bound ligand:
Ligand 8MF 1 x 8MF
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P41212
Unit cell:
a: 69.41Å b: 69.41Å c: 252.159Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.257
Expression system: Escherichia coli K-12

Quick links

Citations

10 review citations

Old and New Approaches to Target the Hsp90 Chaperone.
Sanchez et al. (2020)
9 more

3 mentions without citation

Design and Synthesis of TRAP1 Selective Inhibitors: H-Bonding with Asn171 Residue in TRAP1 Increases Paralog Selectivity.
Yang et al. (2021)
2 more