1JDW

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

Summary for 1JDW

Entry DOI	10.2210/pdb1jdw/pdb
Descriptor	L-ARGININE\:GLYCINE AMIDINOTRANSFERASE, BETA-MERCAPTOETHANOL (3 entities in total)
Functional Keywords	transferase, creatine biosynthesis, catalytic triad, reaction mechanism, novel fold, fivefold pseudosymmetry
Biological source	Homo sapiens (human)
Cellular location	Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side (Potential): P50440
Total number of polymer chains	1
Total formula weight	48599.50
Authors	Humm, A.,Fritsche, E.,Steinbacher, S.,Huber, R. (deposition date: 1997-01-22, release date: 1998-01-28, Last modification date: 2011-07-13)
Primary citation	Humm, A.,Fritsche, E.,Steinbacher, S.,Huber, R. Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. EMBO J., 16:3373-3385, 1997 Cited by PubMed: 9218780 DOI: 10.1093/emboj/16.12.3373 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation