› 3pgx

X-ray diffraction
1.85Å resolution

Crystal structure of a putative carveol dehydrogenase from Mycobacterium paratuberculosis bound to nicotinamide adenine dinucleotide

Released:
DOI: 10.2210/pdb3pgx/pdb
PDB entry 3pgx coloured by chain, front view.
PDB entry 3pgx coloured by chain, side view.
PDB entry 3pgx coloured by chain, top view.
Source organism: Mycobacterium avium subsp. paratuberculosis
Primary publication:
Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors.
Haft DH, Pierce PG, Mayclin SJ, Sullivan A, Gardberg AS, Abendroth J, Begley DW, Phan IQ, Staker BL, Myler PJ, Marathias VM, Lorimer DD, Edwards TE
Sci Rep 7 41074 (2017)
PMID: 28120876

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-180971 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Uncharacterized NAD-dependent oxidoreductase MAP_4146 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 280 amino acids
Theoretical weight: 29.36 KDa
Source organism: Mycobacterium avium subsp. paratuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: Q73SC8 (Residues: 2-275; Coverage: 100%)
Gene name: MAP_4146
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

1 bound ligand:
Ligand NAD 4 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.3
Spacegroup: C2
Unit cell:
a: 130.03Å b: 57.92Å c: 131.74Å
α: 90° β: 91.35° γ: 90°
R-values:
R R work R free
0.147 0.145 0.195
Expression system: Escherichia coli

Quick links

Citations

5 review citations

New developments in RiPP discovery, enzymology and engineering.
Montalbán-López et al. (2021)
4 more

1 mention without citation

Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors.
Haft et al. (2017)