PDBe 1mt1

X-ray diffraction
2.2Å resolution

The Crystal Structure of Pyruvoyl-dependent Arginine Decarboxylase from Methanococcus jannaschii

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Pyruvoyl-dependent arginine decarboxylase subunit beta Chains: A, C, E, G, I, K
Molecule details ›
Chains: A, C, E, G, I, K
Length: 52 amino acids
Theoretical weight: 5.48 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q57764 (Residues: 1-52; Coverage: 32%)
Gene names: MJ0316, pdaD
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1
Pyruvoyl-dependent arginine decarboxylase subunit alpha Chains: B, D, F, H, J, L
Molecule details ›
Chains: B, D, F, H, J, L
Length: 113 amino acids
Theoretical weight: 12.53 KDa
Source organism: Methanocaldococcus jannaschii
Expression system: Escherichia coli
UniProt:
  • Canonical: Q57764 (Residues: 54-165; Coverage: 68%)
Gene names: MJ0316, pdaD
Structure domains: Pyruvoyl-Dependent Histidine Decarboxylase, subunit B

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 8-BM
Spacegroup: P21
Unit cell:
a: 56.77Å b: 92.99Å c: 87.23Å
α: 90° β: 94.84° γ: 90°
R-values:
R R work R free
0.206 0.19 0.229
Expression system: Escherichia coli