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› 4bgk

X-ray diffraction
2.18Å resolution

Three dimensional structure of human gamma-butyrobetaine hydroxylase in complex with (3-(Trimethylammonio)propyl)phosphinate

Released:
DOI: 10.2210/pdb4bgk/pdb
Model geometry
Fit model/data
PDB entry 4bgk coloured by chain, front view.
PDB entry 4bgk coloured by chain, side view.
PDB entry 4bgk coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Targeting carnitine biosynthesis: discovery of new inhibitors against γ-butyrobetaine hydroxylase.
Tars K, Leitans J, Kazaks A, Zelencova D, Liepinsh E, Kuka J, Makrecka M, Lola D, Andrianovs V, Gustina D, Grinberga S, Liepinsh E, Kalvinsh I, Dambrova M, Loza E, Pugovics O
J Med Chem 57 2213-36 (2014)
PMID: 24571165

Function and Biology Details

Reaction catalysed: 
4-(trimethylamino)butanoate + 2-oxoglutarate + O2 = carnitine +succinate + CO2.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131180 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gamma-butyrobetaine dioxygenase Chain: A
Molecule details ›
Chain: A
Length: 387 amino acids
Theoretical weight: 44.77 KDa
Source organism: Homo sapiens
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: O75936 (Residues: 1-387; Coverage: 100%)
Gene names: BBH, BBOX, BBOX1
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand OGA 1 x OGA
Ligand RTK 1 x RTK
Ligand ZN 2 x ZN
Ligand 16D 1 x 16D
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: MAX II BEAMLINE I911-3
Spacegroup: R32
Unit cell:
a: 107.72Å b: 107.72Å c: 204.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.148 0.146 0.194
Expression system: Saccharomyces cerevisiae

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Citations

4 review citations

2-Oxoglutarate-Dependent Oxygenases.
Islam et al. (2018)
3 more