› 7rcm

X-ray diffraction
2.1Å resolution

Crystal Structure of ADP-bound Galactokinase

Released:
DOI: 10.2210/pdb7rcm/pdb
PDB entry 7rcm coloured by chain, front view.
PDB entry 7rcm coloured by chain, side view.
PDB entry 7rcm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure-Based Optimization of Small Molecule Human Galactokinase Inhibitors.
Liu L, Tang M, Pragani R, Whitby FG, Zhang YQ, Balakrishnan B, Fang Y, Karavadhi S, Tao D, LeClair CA, Hall MD, Marugan JJ, Boxer M, Shen M, Hill CP, Lai K, Patnaik S
J Med Chem 64 13551-13571 (2021)
PMID: 34491744

Function and Biology Details

Reaction catalysed: 
ATP + alpha-D-galactose = ADP + alpha-D-galactose 1-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156361 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Galactokinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 392 amino acids
Theoretical weight: 42.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P51570 (Residues: 1-392; Coverage: 100%)
Gene names: GALK, GALK1
Sequence domains:

Ligands and Environments

6 bound ligands:
Ligand ADP 2 x ADP
Ligand GLA 2 x GLA
Ligand PO4 6 x PO4
Ligand MG 2 x MG
Ligand NA 2 x NA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P6122
Unit cell:
a: 128.793Å b: 128.793Å c: 240.652Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.196 0.236
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Galactokinase 1 is the source of elevated galactose-1-phosphate and cerebrosides are modestly reduced in a mouse model of classic galactosemia.
Mangini et al. (2024)

1 mention without citation

Structure-Based Optimization of Small Molecule Human Galactokinase Inhibitors.
Liu et al. (2021)