CRYSTAL STRUCTURE AND MECHANISM OF L-ARGININE: GLYCINE AMIDINOTRANSFERASE: A MITOCHONDRIAL ENZYME INVOLVED IN CREATINE BIOSYNTHESIS
The structure was published by Humm, A., Fritsche, E., Steinbacher, S., and Huber, R., in 1997 in a paper entitled "Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 1997.
The experimental data on which the structure is based was not deposited.
The PDB entry contains the structure of L-ARGININE\:GLYCINE AMIDINOTRANSFERASE. This molecule has the UniProt identifier P50440 (GATM_HUMAN). The sample contained 423 residues which is 100% of the natural sequence. Out of 423 residues 360 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule most likely forms homodimers.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: