4igm

X-ray diffraction
2.39Å resolution

2.39 Angstrom X-ray Crystal structure of human ACMSD

Released:
Source organism: Homo sapiens
Entry authors: Liu F, Liu A

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 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 332 amino acids
Theoretical weight: 37.55 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 89.112Å b: 101.878Å c: 233.455Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.208 0.29
Expression system: Escherichia coli