› 5lti

X-ray diffraction
1.9Å resolution

Crystal structure of the alpha subunit of heme dependent oxidative N-demethylase (HODM) in complex with the dimethylamine substrate

Released:
DOI: 10.2210/pdb5lti/pdb
PDB entry 5lti coloured by chain, front view.
PDB entry 5lti coloured by chain, side view.
PDB entry 5lti coloured by chain, top view.
Source organism: Pseudomonas mendocina
Primary publication:
An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme.
Ortmayer M, Lafite P, Menon BR, Tralau T, Fisher K, Denkhaus L, Scrutton NS, Rigby SE, Munro AW, Hay S, Leys D
Nature 539 593-597 (2016)
PMID: 27851736

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107491 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DUF3445 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 344 amino acids
Theoretical weight: 40.16 KDa
Source organism: Pseudomonas mendocina
Expression system: Escherichia coli
UniProt:
  • Canonical: A4XXY9 (Residues: 1-338; Coverage: 100%)
Gene name: Pmen_3455
Sequence domains: Haem-dependent oxidative N-demethylase, alpha subunit-like

Ligands and Environments

5 bound ligands:
Ligand HEM 1 x HEM
Ligand DMN 1 x DMN
Ligand NO 1 x NO
Ligand PEG 1 x PEG
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P43212
Unit cell:
a: 80.212Å b: 80.212Å c: 144.608Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.173 0.201
Expression system: Escherichia coli

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Citations

2 review citations

Harnessing Conformational Plasticity to Generate Designer Enzymes.
Crean et al. (2020)
1 more