› 2n6d

Solution NMR

NMR structure of the 140-315 fragment of the N-acetylglucosamine-1-phosphate transferase, alpha and beta subunits

Released:
DOI: 10.2210/pdb2n6d/pdb
PDB entry 2n6d coloured by chain, ensemble of 19 models, front view.
PDB entry 2n6d coloured by chain, ensemble of 19 models, side view.
PDB entry 2n6d coloured by chain, ensemble of 19 models, top view.
Source organism: Homo sapiens
Entry authors: Serrano P, Geralt M, Wuthrich K, Joint Center for Structural Genomics (JCSG)

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
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-174806 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylglucosamine-1-phosphotransferase subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 172 amino acids
Theoretical weight: 19.16 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q3T906 (Residues: 134-305; Coverage: 14%)
Gene names: GNPTA, GNPTAB, KIAA1208
Sequence domains: Putative GlcNAc-1 phosphotransferase regulatory domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 87%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

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