› 3oec

X-ray diffraction
1.95Å resolution

Crystal structure of carveol dehydrogenase from Mycobacterium thermoresistibile

Released:
DOI: 10.2210/pdb3oec/pdb
PDB entry 3oec coloured by chain, front view.
PDB entry 3oec coloured by chain, side view.
PDB entry 3oec coloured by chain, top view.
Source organism: Mycolicibacterium thermoresistibile
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

Reaction catalysed: 
(2S)-flavan-4-ol + NADP(+) = (2S)-flavanone + NADPH
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-122785 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carveol dehydrogenase (MythA.01326.c, A0R518 homolog) Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 317 amino acids
Theoretical weight: 34.28 KDa
Source organism: Mycolicibacterium thermoresistibile
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E1C9L4 (Residues: 1-309; Coverage: 100%)
Sequence domains: short chain dehydrogenase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: C2
Unit cell:
a: 67.86Å b: 120.57Å c: 134.56Å
α: 90° β: 94.05° γ: 90°
R-values:
R R work R free
0.179 0.176 0.233
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

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

2 mentions without citation

Biochemical studies and ligand-bound structures of biphenyl dehydrogenase from Pandoraea pnomenusa strain B-356 reveal a basis for broad specificity of the enzyme.
Dhindwal et al. (2011)
1 more