9jer

X-ray diffraction
1.9Å resolution

Arginine decarboxylase in Aspergillus oryzae, ligand-free form

Released:

Function and Biology Details

Reaction catalysed:
L-arginine = agmatine + CO(2)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-274685 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
L-tryptophan decarboxylase PsiD-like domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 462 amino acids
Theoretical weight: 51.17 KDa
Source organism: Aspergillus oryzae RIB40
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q2UAM5 (Residues: 1-442; Coverage: 92%)
Gene name: AO090102000327
Sequence domains:
L-tryptophan decarboxylase PsiD-like domain-containing protein Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 42 amino acids
Theoretical weight: 4.68 KDa
Source organism: Aspergillus oryzae RIB40
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q2UAM5 (Residues: 443-483; Coverage: 9%)
Gene name: AO090102000327

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: C2221
Unit cell:
a: 134.692Å b: 196.484Å c: 196.783Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.169 0.202
Expression system: Escherichia coli BL21