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Structure paper

TitleCrystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis.
Journal, issue, pagesEMBO J., Vol. 16, Page 3373-3385, Year 1997
Publish dateJan 22, 1997 (structure data deposition date)
AuthorsHumm, A. / Fritsche, E. / Steinbacher, S. / Huber, R.
External linksEMBO J. / PubMed:9218780
MethodsX-ray diffraction
Resolution1.9 - 2.5 Å
Structure data

PDB-1jdw:
CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-2jdw:
CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

PDB-3jdw:
CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

PDB-4jdw:
CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

Chemicals

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-HOH:
WATER

ChemComp-ORN:
L-ornithine

ChemComp-ARG:
ARGININE

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / CREATINE BIOSYNTHESIS / CATALYTIC TRIAD / REACTION MECHANISM / NOVEL FOLD / FIVEFOLD PSEUDOSYMMETRY

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