Structure of PDB 6xi2 Chain D Binding Site BS01

Receptor Information

>6xi2 Chain D (length=521) Species: 9606 (Homo sapiens)

ALRIDYPAALQILMEGGTHMVCTGRTHTDRICRFKWLCYSNEAEEFIFFH
GNTSVMLPNLGSRRFQPALLDLSTVEDHNTQYFNFVELPAAALRFMPKPV
FVPDVALIANRFNPDNLMHVFHDDLLPLFYTLRQFPGLAHEARLFFMEGW
GEGAHFDLYKLLSPKQPLLRAQLKTLGRLLCFSHAFVGLSKITTWYQYGF
VQPQGPKANILVSGNEIRQFARFMTEKLNASAAEYILVFARTQNRLILNE
AELLAALAQEFQMKTVTVSLEDHTFADVVRLVSNASMLVSMHGAQLVTTL
FLPRGATVVELFPYAVNPDHYTPYKTLAMLPGMDLQYVAWRNMMPENTVT
HPERPWDQGGITHLDRAEQARILSSREVPRHLCCRNPEWLFRIYQDTKVD
IPSLIQTIRRVVAGAPGPAGLYPGKVREARCQASVHGASEARLTVSWQIP
WNLKYLKVAEVKYEVWLQEAGENTYVPYILALQNHTFTENIKPFTTYLVW
VRCIFNKILLGPFADVLVCNT

Ligand information

>6xi2 Chain G (length=10) Species: 9606 (Homo sapiens)

AAAAAAAAAA

Receptor-Ligand Complex Structure

Structure summary

• PDB: 6xi2 Crystal structures of beta-1,4-N-acetylglucosaminyltransferase 2: structural basis for inherited muscular dystrophies.
• Resolution: 2.57 Å
• Binding residue (original residue number in PDB): Y53 V147 F148
• Binding residue (residue number reindexed from 1): Y6 V100 F101

Enzymatic activity

• Enzyme Commision number: 2.4.1.312: protein O-mannose beta-1,4-N-acetylglucosaminyltransferase.

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

External links

• PDB: RCSB:6xi2, PDBe:6xi2, PDBj:6xi2
• PDBsum: 6xi2
• PubMed: 33825709
• UniProt: Q8NAT1|PMGT2_HUMAN Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2 (Gene Name=POMGNT2)