› 8jdw

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF HUMAN L-ARGININE:GLYCINE AMIDINOTRANSFERASE IN COMPLEX WITH L-ALANINE

Released:
DOI: 10.2210/pdb8jdw/pdb
PDB entry 8jdw coloured by chain, front view.
PDB entry 8jdw coloured by chain, side view.
PDB entry 8jdw coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The ligand-induced structural changes of human L-Arginine:Glycine amidinotransferase. A mutational and crystallographic study.
Fritsche E, Humm A, Huber R
J Biol Chem 274 3026-32 (1999)
PMID: 9915841

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)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycine amidinotransferase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 386 amino acids
Theoretical weight: 44.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P50440 (Residues: 38-423; Coverage: 91%)
Gene names: AGAT, GATM
Structure domains: L-arginine/glycine Amidinotransferase; Chain A

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 83.76Å b: 83.76Å c: 199.95Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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

2 mentions without citation

Mechanistic similarity and diversity among the guanidine-modifying members of the pentein superfamily.
Linsky et al. (2010)
1 more