Structure of PDB 6xi2 Chain D

Receptor sequence
>6xi2D (length=521) Species: 9606 (Homo sapiens) [Search protein sequence]
ALRIDYPAALQILMEGGTHMVCTGRTHTDRICRFKWLCYSNEAEEFIFFH
GNTSVMLPNLGSRRFQPALLDLSTVEDHNTQYFNFVELPAAALRFMPKPV
FVPDVALIANRFNPDNLMHVFHDDLLPLFYTLRQFPGLAHEARLFFMEGW
GEGAHFDLYKLLSPKQPLLRAQLKTLGRLLCFSHAFVGLSKITTWYQYGF
VQPQGPKANILVSGNEIRQFARFMTEKLNASAAEYILVFARTQNRLILNE
AELLAALAQEFQMKTVTVSLEDHTFADVVRLVSNASMLVSMHGAQLVTTL
FLPRGATVVELFPYAVNPDHYTPYKTLAMLPGMDLQYVAWRNMMPENTVT
HPERPWDQGGITHLDRAEQARILSSREVPRHLCCRNPEWLFRIYQDTKVD
IPSLIQTIRRVVAGAPGPAGLYPGKVREARCQASVHGASEARLTVSWQIP
WNLKYLKVAEVKYEVWLQEAGENTYVPYILALQNHTFTENIKPFTTYLVW
VRCIFNKILLGPFADVLVCNT
3D structure
PDB6xi2 Crystal structures of beta-1,4-N-acetylglucosaminyltransferase 2: structural basis for inherited muscular dystrophies.
ChainD
Resolution2.57 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 peptide D Y53 V147 F148 Y6 V100 F101
Gene Ontology
Molecular Function
GO:0005515 protein binding
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:6xi2, PDBe:6xi2, PDBj:6xi2
PDBsum6xi2
PubMed33825709
UniProtQ8NAT1|PMGT2_HUMAN Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 (Gene Name=POMGNT2)

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