Structure of PDB 7e9j Chain B

Receptor sequence
>7e9jB (length=521) Species: 9913 (Bos taurus) [Search protein sequence]
DYPKALQILTEGGTHMVCTGRTHTDRLCRFKWLCYSSEAEEFIFFHGNAS
VMLPSLGSRRFQPALLDLSTVEDHNTQYFNFVELPAAALRFMPKPVFVPD
VALIANRFNPDNLMHVFHDDLLPLFYTLRQFPGLAREARLFFMEGWGEGA
HFDLYKLLSPKQPLLRAQLKALGRLLCFSHAFVGLSKVTTWYQYGFVQPQ
GPKANILVSGNEIRQFAHFLMEKLNVEEYILVFSRTQNRLILNEAELLLA
LAQEFQMKTVTVSLEDHAFADVVRLVSNASMLVSMHGAQLVTALFLPRGA
AVVELFPYAVNPDHYTPYKTLATLPGMDLQYIAWQNTMPENTVTHPERPW
DQGGIAHLDRAEQARILQSREVPRHLCCRNPEWLFRIYQDTKVDIPSLIQ
TIRRVVKGHPGPRKQKWTVSLYPGKVREARCQASVQGASEARLSVSWQIP
WNLKYLKVREVKYEVWLQEQGENTYVPYMLALQNHTFTENIKPFTTYLVW
IRCIFNKTLLGPFADVLVCST
3D structure
PDB7e9j The structure of POMGNT2 provides new insights into the mechanism to determine the functional O-mannosylation site on alpha-dystroglycan.
ChainB
Resolution2.4 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.312: protein O-mannose beta-1,4-N-acetylglucosaminyltransferase.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 UDP B N163 L164 R294 Q296 N297 R298 L323 A347 Y447 N112 L113 R235 Q237 N238 R239 L264 A288 Y388
Gene Ontology
Molecular Function
GO:0008375 acetylglucosaminyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0097363 protein O-acetylglucosaminyltransferase activity
Biological Process
GO:0001764 neuron migration
GO:0006486 protein glycosylation
GO:0006493 protein O-linked glycosylation
GO:0035269 protein O-linked mannosylation
Cellular Component
GO:0005783 endoplasmic reticulum
GO:0005789 endoplasmic reticulum membrane
GO:0016020 membrane

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Molecular Function

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Biological Process

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Cellular Component
External links
PDB RCSB:7e9j, PDBe:7e9j, PDBj:7e9j
PDBsum7e9j
PubMed33893702
UniProtQ5NDF2|PMGT2_BOVIN Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 (Gene Name=POMGNT2)

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