4x9l

X-ray diffraction
3.1Å resolution

N-terminal domain of Heat shock protein 90 from Oryza sativa

Released:
Source organism: Oryza sativa Japonica Group
Primary publication:
Functional characterization of heat-shock protein 90 from Oryza sativa and crystal structure of its N-terminal domain.
Acta Crystallogr F Struct Biol Commun 71 688-96 (2015)
PMID: 26057797

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein 81-3 Chain: A
Molecule details ›
Chain: A
Length: 250 amino acids
Theoretical weight: 27.77 KDa
Source organism: Oryza sativa Japonica Group
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q07078 (Residues: 1-216; Coverage: 31%)
Gene names: HSP81-3, LOC_Os09g30418, Os09g0482400, Os09g0482600, P0463D04.35
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: I422
Unit cell:
a: 116.87Å b: 116.87Å c: 105.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.245 0.292
Expression system: Escherichia coli BL21(DE3)