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

X-ray diffraction
1.9Å resolution
PDB entry 1jdw coloured by chain, front view.
PDB entry 1jdw coloured by chain, side view.
PDB entry 1jdw coloured by chain, top view.
Source organism: Homo sapiens
Assembly composition:
homo dimer (preferred)
Entry contents: 1 distinct polypeptide molecule

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Assemblies

Assembly 1 (preferred)
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Assembly Name: Glycine amidinotransferase, mitochondrial
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Multimeric state: homo dimer
Accessible surface area: 23886.44 Å2
Buried surface area: 3467.14 Å2
Dissociation area: 1,473.39 Å2
Dissociation energy (ΔGdiss): 4.22 kcal/mol
Dissociation entropy (TΔSdiss): 13.93 kcal/mol
Symmetry number: 2
PDBe Complex ID: PDB-CPX-156180

Macromolecules

Glycine amidinotransferase, mitochondrial
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
Glycine amidinotransferase, mitochondrial in PDB entry 1jdw, assembly 1, front view.
Glycine amidinotransferase, mitochondrial in PDB entry 1jdw, assembly 1, side view.
Glycine amidinotransferase, mitochondrial in PDB entry 1jdw, assembly 1, top view.
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