Structure analysis

CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS

X-ray diffraction
1.9Å resolution
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

Assemblies

Assembly 1 (preferred)
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Multimeric state: homo dimer
Accessible surface area: 23900 Å2
Buried surface area: 3500 Å2
Dissociation area: 1,500 Å2
Dissociation energy (ΔGdiss): 3 kcal/mol
Dissociation entropy (TΔSdiss): 14 kcal/mol
Interface energy (ΔGint): -11 kcal/mol
Symmetry number: 2

Macromolecules

Chain: A
Length: 423 amino acids
Theoretical weight: 48.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50440 (Residues: 1-423; Coverage: 100%)
Gene names: AGAT, GATM
InterPro: Glycine/inosamine-phosphate amidinotransferase
CATH: L-arginine/glycine Amidinotransferase; Chain A
SCOP: Amidinotransferase

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