› 4ifr

X-ray diffraction
2.39Å resolution

2.40 Angstroms X-ray crystal structure of R239A 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase from Pseudomonas fluorescens

Released:
DOI: 10.2210/pdb4ifr/pdb
PDB entry 4ifr coloured by chain, front view.
PDB entry 4ifr coloured by chain, side view.
PDB entry 4ifr 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182963 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amidohydrolase-related domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 330 amino acids
Theoretical weight: 36.61 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83V25 (Residues: 4-333; 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-ID
Spacegroup: P42212
Unit cell:
a: 91.162Å b: 91.162Å c: 167.989Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.214 0.21 0.295
Expression system: Escherichia coli BL21(DE3)

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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)