› 2hbv

X-ray diffraction
1.65Å resolution

Crystal Structure of alpha-Amino-beta-Carboxymuconate-epsilon-Semialdehyde-Decarboxylase (ACMSD)

Released:
DOI: 10.2210/pdb2hbv/pdb
PDB entry 2hbv coloured by chain, front view.
PDB entry 2hbv coloured by chain, side view.
PDB entry 2hbv coloured by chain, top view.
Source organism: Pseudomonas fluorescens
Primary publication:
Crystal structure of alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase: insight into the active site and catalytic mechanism of a novel decarboxylation reaction.
Martynowski D, Eyobo Y, Li T, Yang K, Liu A, Zhang H
Biochemistry 45 10412-21 (2006)
PMID: 16939194

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 domain:

Structure analysis Details

Assemblies composition:
homo dimer (preferred)
homo tetramer
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: 334 amino acids
Theoretical weight: 37.18 KDa
Source organism: Pseudomonas fluorescens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q83V25 (Residues: 1-334; Coverage: 100%)
Gene name: nbaD
Sequence domains: Amidohydrolase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 153.557Å b: 48.107Å c: 110.7Å
α: 90° β: 127.31° γ: 90°
R-values:
R R work R free
0.251 0.211 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Asymmetric catalysis with chiral primary amine-based organocatalysts.
Xu et al. (2009)
3 more

10 mentions without citation

Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis.
Khare et al. (2012)
9 more