› 4ig2

X-ray diffraction
1.8Å resolution

1.80 Angstroms X-ray crystal structure of R51A and R239A heterodimer 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase from Pseudomonas fluorescens

Released:
DOI: 10.2210/pdb4ig2/pdb
PDB entry 4ig2 coloured by chain, front view.
PDB entry 4ig2 coloured by chain, side view.
PDB entry 4ig2 coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
The power of two: arginine 51 and arginine 239* from a neighboring subunit are essential for catalysis in α-amino-β-carboxymuconate-epsilon-semialdehyde decarboxylase.
Huo L, Davis I, Chen L, Liu A
J Biol Chem 288 30862-71 (2013)
PMID: 24019523

Function and Biology Details

Reaction catalysed: 
2-amino-3-(3-oxoprop-1-en-1-yl)but-2-enedioate = 2-aminomuconate semialdehyde + CO(2)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182962 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Amidohydrolase-related domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 331 amino acids
Theoretical weight: 36.74 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83V25 (Residues: 3-333; Coverage: 99%)
Gene name: nbaD
Sequence domains: Amidohydrolase
Structure domains: Metal-dependent hydrolases
Amidohydrolase-related domain-containing protein Chain: B
Molecule details ›
Chain: B
Length: 331 amino acids
Theoretical weight: 36.74 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q83V25 (Residues: 3-333; Coverage: 99%)
Gene name: nbaD
Sequence domains: Amidohydrolase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: C2
Unit cell:
a: 153.101Å b: 48.523Å c: 109.829Å
α: 90° β: 126.8° γ: 90°
R-values:
R R work R free
0.234 0.232 0.282
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli

Quick links

Citations

1 review citation

Structural insights into the half-of-sites reactivity in homodimeric and homotetrameric metalloenzymes.
Nguyen et al. (2023)
14 other articles

1 mention without citation

The power of two: arginine 51 and arginine 239* from a neighboring subunit are essential for catalysis in α-amino-β-carboxymuconate-epsilon-semialdehyde decarboxylase.
Huo et al. (2013)