7sj2

X-ray diffraction
2.3Å resolution

N-acetylglucosamine-1-phosphotransferase (GNPT) alpha and beta subunits (GNPTAB) catalytic domain, from zebrafish, in complex with uridine diphosphate N-acetylglucosamine (UDP-GlcNAc) and magnesium

Released:
Entry authors: Gorelik A, Illes K, Nagar B

Function and Biology Details

Reaction catalysed:
UDP-N-acetyl-D-glucosamine + lysosomal-enzyme D-mannose = UMP + lysosomal-enzyme N-acetyl-D-glucosaminyl-phospho-D-mannose
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (5 distinct):
LNR domain-containing protein; N-acetylglucosamine-1-phosphotransferase subunit beta Chains: A, B
Molecule details ›
Chains: A, B
Length: 495 amino acids
Theoretical weight: 58.36 KDa
Source organisms: Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q54MP1 (Residues: 61-86, 87-258; Coverage: 16%)
  • Canonical: Q5RGJ8 (Residues: 894-1173; Coverage: 23%)
Gene names: DDB0186697, gnpta, gnptab, si:ch211-234f20.3, zgc:122985
Sequence domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer : NEW Components: NAG, BMA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P21
Unit cell:
a: 94.542Å b: 87.142Å c: 108.369Å
α: 90° β: 111.858° γ: 90°
R-values:
R R work R free
0.162 0.16 0.202
Expression system: Spodoptera frugiperda