5GGL: PDB entry 5GGL

Crystal structure of N-terminal domain of human protein O-mannose beta-1,2-N-acetylglucosaminyltransferase in complex with GlcNAc-alpha-pNP. Determined by X-ray diffraction at 1.27 Å resolution. Released 10 Aug 2016.

Method
X-ray diffraction
Resolution
1.27 Å
Organism
Homo sapiens
Chains
2
Atoms
2,665
Mol. weight
35.93 kDa
Ligands
6ZC
Released
10 Aug 2016

Explore 5GGL in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5GGL contains 9 α-helices and 20 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 4 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand98-10581
β-strand10612
β-strand110-11451
β-strand117-12261
β-strand130-13672
β-strand143-14972
α-helix156-16611
β-strand172-17872
α-helix187-1959
α-helix201-2033
β-strand209-21572
β-strand220-22672
α-helix235-2373
β-strand238-24581
Chain B: 5 helices, 10 β-strands
ElementResiduesLengthSheet
β-strand99-10573
β-strand10614
β-strand110-11453
β-strand117-12263
β-strand130-13674
β-strand143-14974
α-helix156-16611
α-helix1681
β-strand172-17874
α-helix187-1959
α-helix201-2033
β-strand209-21574
β-strand220-22674
α-helix235-2373
β-strand238-24473

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1A, Bprotein164Homo sapiensQ8WZA1 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5GGL_1 Protein O-linked-mannose beta-1,2-N-acetylglucosaminyltransferase 1 (chains A, B)
GPLGSGSGPRRVLDVEVYSSRSKVYVAVDGTTVLEDEAREQGRGIHVIVLNQATGHVMAK
RVFDTYSPHEDEAMVLFLNMVAPGRVLICTVKDEGSFHLKDTAKALLRSLGSQAGPALGW
RDTWAFVGRKGGPVFGEKHSKSPALSSWGDPVLLKTDVPLSSAE

Ligands and cofactors

IDNameFormulaCopies
6ZC4-nitrophenyl 2-acetamido-2-deoxy-alpha-D-glucopyranosideC14 H18 N2 O82

Primary citation

Carbohydrate-binding domain of the POMGnT1 stem region modulates O-mannosylation sites of alpha-dystroglycan. Kuwabara, N., Manya, H., Yamada, T. et al. Proc Natl Acad Sci U S A (2016) 113:9280-9285. DOI 10.1073/pnas.1525545113 · PubMed

Other PDB entries of the same protein (UniProt Q8WZA1 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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