› 4ign

X-ray diffraction
2.33Å resolution

2.32 Angstrom X-ray Crystal structure of R47A mutant of human ACMSD

Released:
DOI: 10.2210/pdb4ign/pdb
PDB entry 4ign coloured by chain, front view.
PDB entry 4ign coloured by chain, side view.
PDB entry 4ign coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): a structural and mechanistic unveiling.
Huo L, Liu F, Iwaki H, Li T, Hasegawa Y, Liu A
Proteins 83 178-87 (2015)
PMID: 25392945

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-186215 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 332 amino acids
Theoretical weight: 37.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8TDX5 (Residues: 1-332; Coverage: 99%)
Gene name: ACMSD
Sequence domains: Amidohydrolase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

1 bound ligand:
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 89.142Å b: 101.686Å c: 232.613Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.276
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Is the Enzyme ACMSD a Novel Therapeutic Target in Parkinson's Disease?
Thirtamara-Rajamani et al. (2017)
2 more

3 mentions without citation

Human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD): a structural and mechanistic unveiling.
Huo et al. (2015)
2 more