Structure analysis

Crystal Structure of THEP1 from the hyperthermophile Aquifex aeolicus

X-ray diffraction
1.4Å resolution
Source organism: Aquifex aeolicus
Assembly composition:
monomeric (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: monomeric
Accessible surface area: 8700 Å2
Buried surface area: 700 Å2
Dissociation area: 100 Å2
Dissociation energy (ΔGdiss): 14 kcal/mol
Dissociation entropy (TΔSdiss): -1 kcal/mol
Interface energy (ΔGint): -44 kcal/mol
Symmetry number: 1

Macromolecules

Chain: A
Length: 178 amino acids
Theoretical weight: 20.73 KDa
Source organism: Aquifex aeolicus
Expression system: Escherichia coli
UniProt:
  • Canonical: O67322 (Residues: 1-178; Coverage: 100%)
Gene name: aq_1292
Pfam: NTPase
InterPro:
CATH: P-loop containing nucleotide triphosphate hydrolases
SCOP: RecA protein-like (ATPase-domain)

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