› 3jdw

X-ray diffraction
2.4Å resolution

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

Released:
DOI: 10.2210/pdb3jdw/pdb
PDB entry 3jdw coloured by chain, front view.
PDB entry 3jdw coloured by chain, side view.
PDB entry 3jdw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure and mechanism of human L-arginine:glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis.
Humm A, Fritsche E, Steinbacher S, Huber R
EMBO J 16 3373-85 (1997)
PMID: 9218780

Function and Biology Details

Reaction catalysed: 
L-arginine + glycine = L-ornithine + guanidinoacetate
Biochemical function:
Biological process:
Cellular component:
Sequence domain:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine amidinotransferase, mitochondrial Chain: A
Molecule details ›
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
Structure domains: L-arginine/glycine Amidinotransferase; Chain A

Ligands and Environments

1 bound ligand:
Ligand ORN 1 x ORN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P43212
Unit cell:
a: 83.76Å b: 83.76Å c: 199.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 not available
Expression system: Escherichia coli

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Citations

11 review citations

Creatine and creatinine metabolism.
Wyss et al. (2000)
10 more