› 9azo

X-ray diffraction
2.34Å resolution

Crystal structure of CHMS Dehydrogenase PmdC from Comamonas testosteroni bound to cofactor NADP

Released:
DOI: 10.2210/pdb9azo/pdb
PDB entry 9azo coloured by chain, front view.
PDB entry 9azo coloured by chain, side view.
PDB entry 9azo coloured by chain, top view.
Source organism: Comamonas testosteroni ATCC 11996
Primary publication:
Characterization of lignin degrading enzyme PmdC, which catalyzes a key step in the synthesis of polymer precursor 2-pyrone-4,6-dicarboxylic acid (PDC).
Rodrigues AV, Moriarty NW, Kakumanu R, DeGiovanni A, Pereira JH, Gin JW, Chen Y, Baidoo EEK, Petzold CJ, Adams PD
J Biol Chem 107736 (2024)
PMID: 39222681

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-572004 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
PmdC Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 319 amino acids
Theoretical weight: 35.25 KDa
Source organism: Comamonas testosteroni ATCC 11996
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q93PS4 (Residues: 1-319; Coverage: 100%)
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 7 x SO4
Ligand NAP 6 x NAP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS-II BEAMLINE 17-ID-2, ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 79.151Å b: 157.864Å c: 95.011Å
α: 90° β: 114.449° γ: 90°
R-values:
R R work R free
0.24 0.239 0.277
Expression system: Escherichia coli BL21(DE3)

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