› 2a2c

X-ray diffraction
1.65Å resolution

x-ray structure of human N-acetyl galactosamine kinase complexed with Mg-ADP and N-acetyl galactosamine 1-phosphate

Released:
DOI: 10.2210/pdb2a2c/pdb
PDB entry 2a2c coloured by chain, front view.
PDB entry 2a2c coloured by chain, side view.
PDB entry 2a2c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The molecular architecture of human N-acetylgalactosamine kinase.
Thoden JB, Holden HM
J Biol Chem 280 32784-91 (2005)
PMID: 16006554

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-169555 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylgalactosamine kinase Chain: A
Molecule details ›
Chain: A
Length: 478 amino acids
Theoretical weight: 52.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q01415 (Residues: 1-458; Coverage: 100%)
Gene names: GALK2, GK2
Sequence domains:
Structure domains:

Ligands and Environments

5 bound ligands:
Ligand NG1 1 x NG1
Ligand MG 1 x MG
Ligand CL 1 x CL
Ligand NA 1 x NA
Ligand ADP 1 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P65
Unit cell:
a: 123.8Å b: 123.8Å c: 60.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.168 0.167 0.201
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Metabolic glycoengineering: sialic acid and beyond.
Du et al. (2009)
2 more

3 mentions without citation

The dipeptidyl peptidase IV inhibitors vildagliptin and K-579 inhibit a phospholipase C: a case of promiscuous scaffolds in proteins.
Chakraborty et al. (2013)
2 more