5gz8

X-ray diffraction
2.5Å resolution

Crystal structure of catalytic domain of Protein O-mannosyl Kinase in ligand-free form

Released:

Function and Biology Details

Reaction catalysed:
ATP + O(3)-(N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-mannosyl)-L-threonyl/L-seryl-[protein] = ADP + O(3)-(N-acetyl-beta-D-galactosaminyl-(1->3)-N-acetyl-beta-D-glucosaminyl-(1->4)-alpha-D-(6-phospho)mannosyl)-L-threonyl/L-seryl-[protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-174820 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein O-mannose kinase Chain: A
Molecule details ›
Chain: A
Length: 305 amino acids
Theoretical weight: 35.21 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
UniProt:
  • Canonical: Q3TUA9 (Residues: 45-349; Coverage: 87%)
Gene names: Pomk, Sgk196
Sequence domains: Protein tyrosine and serine/threonine kinase
Structure domains: Transferase(Phosphotransferase) domain 1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NE3A
Spacegroup: P3121
Unit cell:
a: 81.885Å b: 81.885Å c: 147.745Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.274 0.273 0.293
Expression system: Homo sapiens