Structure analysis

Crystal structure of the amino acid kinase domain from Saccharomyces cerevisiae acetylglutamate kinase complexed with its substrate N- acetylglutamate

X-ray diffraction
2.2Å resolution
Source organism: Saccharomyces cerevisiae
Assembly composition:
homo tetramer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo tetramer
Accessible surface area: 45900 Å2
Buried surface area: 15700 Å2
Dissociation area: 5,200 Å2
Dissociation energy (ΔGdiss): -4 kcal/mol
Dissociation entropy (TΔSdiss): 55 kcal/mol
Interface energy (ΔGint): -253 kcal/mol
Symmetry number: 1

Macromolecules

Chains: A, B, C, D
Length: 307 amino acids
Theoretical weight: 34.02 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q01217 (Residues: 58-356; Coverage: 35%)
Gene names: ARG5,6, YER069W
Pfam: Amino acid kinase family
InterPro:
CATH: Acetylglutamate kinase-like

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