2wm1

X-ray diffraction
2.01Å resolution

The crystal structure of human alpha-amino-beta-carboxymuconate- epsilon-semialdehyde decarboxylase in complex with 1,3- dihydroxyacetonephosphate suggests a regulatory link between NAD synthesis and glycolysis

Released:

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:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-186215 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-amino-3-carboxymuconate-6-semialdehyde decarboxylase Chain: A
Molecule details ›
Chain: A
Length: 336 amino acids
Theoretical weight: 38.08 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q8TDX5 (Residues: 1-336; Coverage: 100%)
Gene name: ACMSD
Sequence domains: Amidohydrolase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P3221
Unit cell:
a: 86.227Å b: 86.227Å c: 92.168Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.193 0.257
Expression system: Komagataella pastoris