PDBe 2tmd

X-ray diffraction
2.4Å resolution

CORRELATION OF X-RAY DEDUCED AND EXPERIMENTAL AMINO ACID SEQUENCES OF TRIMETHYLAMINE DEHYDROGENASE

Released:

Function and Biology Details

Reaction catalysed:
Trimethylamine + H(2)O + electron-transferring flavoprotein = dimethylamine + formaldehyde + reduced electron-transferring flavoprotein. 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trimethylamine dehydrogenase Chains: A, B
Molecule details ›
Chains: A, B
Length: 729 amino acids
Theoretical weight: 81.61 KDa
Source organism: Methylophilus methylotrophus W3A1
Expression system: Not provided
UniProt:
  • Canonical: P16099 (Residues: 2-730; Coverage: 100%)
Gene name: tmd
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 147.75Å b: 71.95Å c: 83.82Å
α: 90° β: 97.69° γ: 90°
R-values:
R R work R free
0.154 0.154 not available
Expression system: Not provided