› 2a2d

X-ray diffraction
2.2Å resolution

X-ray structure of human n-acetyl galactosamine kinase complexed with Mn-AMPPNP and n-acetyl glactosamine

Released:
DOI: 10.2210/pdb2a2d/pdb
PDB entry 2a2d coloured by chain, front view.
PDB entry 2a2d coloured by chain, side view.
PDB entry 2a2d 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

3 bound ligands:
Ligand A2G 1 x A2G
Ligand MN 1 x MN
Ligand ANP 1 x ANP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P65
Unit cell:
a: 119.1Å b: 119.1Å c: 65.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.203 0.247
Expression system: Escherichia coli

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Citations

3 review citations

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

2 mentions without citation

Predicting new indications for approved drugs using a proteochemometric method.
Dakshanamurthy et al. (2012)
1 more