Structure of PDB 6iwq Chain D

Receptor sequence
>6iwqD (length=546) Species: 9606 (Homo sapiens) [Search protein sequence]
YLTFKPQTFTYHDPVLRPGILGNFEPKEPEPPGVVGGPGEKAKPLVLGPE
FKQAIQASIKEFGFNMVASDMISLDRSVNDLRQEECKYWHYDENLLTSSV
VIVFHNEGWSTLMRTVHSVIKRTPRKYLAEIVLIDDFSNKEHLKEKLDEY
IKLWNGLVKVFRNERREGLIQARSIGAQKAKLGQVLIYLDAHCEVAVNWY
APLVAPISKDRTICTVPLIDVINGNTYEIIPQGGGDEDGYARGAWDWSML
WKRVPLTPQEKRLRKTKTEPYRSPAMAGGLFAIEREFFFELGLYDPGLQI
WGGENFEISYKIWQCGGKLLFVPCSRVGHIYRLEGWQGNPPPIYVGSSPT
LKNYVRVVEVWWDEYKDYFYASRPESQALPYGDISELKKFREDHNCKSFK
WFMEEIAYDITSHYPLPPKNVDWGEIRGFETAYCIDSMGKTNGGFVELGP
CHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHCNLNEFKEWQYF
KNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNNIHSV
3D structure
PDB6iwq Structural basis of carbohydrate transfer activity of UDP-GalNAc: Polypeptide N-acetylgalactosaminyltransferase 7.
ChainD
Resolution2.95 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 2.4.1.41: polypeptide N-acetylgalactosaminyltransferase.
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 MN D D301 H440 D190 H329
Gene Ontology
Molecular Function
GO:0004653 polypeptide N-acetylgalactosaminyltransferase activity
GO:0016757 glycosyltransferase activity
GO:0030246 carbohydrate binding
GO:0046872 metal ion binding
Biological Process
GO:0005975 carbohydrate metabolic process
GO:0006486 protein glycosylation
GO:0006493 protein O-linked glycosylation
GO:0016266 O-glycan processing
Cellular Component
GO:0000139 Golgi membrane
GO:0005794 Golgi apparatus
GO:0016020 membrane
GO:0070062 extracellular exosome

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:6iwq, PDBe:6iwq, PDBj:6iwq
PDBsum6iwq
PubMed30685086
UniProtQ86SF2|GALT7_HUMAN N-acetylgalactosaminyltransferase 7 (Gene Name=GALNT7)

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