› 4gvx

X-ray diffraction
1.5Å resolution

Crystal structure of a short chain dehydrogenase homolog (target EFI-505321) from burkholderia multivorans, with bound NADP and L-fucose

Released:
DOI: 10.2210/pdb4gvx/pdb
PDB entry 4gvx coloured by chain, front view.
PDB entry 4gvx coloured by chain, side view.
PDB entry 4gvx coloured by chain, top view.
Source organism: Burkholderia multivorans ATCC 17616
Entry authors: Vetting MW, Hobbs ME, Morisco LL, Wasserman SR, Sojitra S, Imker HJ, Raushel FM, Gerlt JA, Almo SC, Enzyme Function Initiative (EFI)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102063 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-fucose dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 258 amino acids
Theoretical weight: 27.71 KDa
Source organism: Burkholderia multivorans ATCC 17616
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H3KNE7 (Residues: 1-258; Coverage: 100%)
Gene name: BMULJ_04919
Sequence domains: Enoyl-(Acyl carrier protein) reductase
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

5 bound ligands:
Ligand NAP 4 x NAP
Ligand CL 4 x CL
Ligand FUL 4 x FUL
Ligand MG 1 x MG
Ligand EDO 7 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: C2
Unit cell:
a: 68.437Å b: 118.522Å c: 118.283Å
α: 90° β: 92.92° γ: 90°
R-values:
R R work R free
0.153 0.152 0.179
Expression system: Escherichia coli

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