5NQA

Crystal structure of GalNAc-T4 in complex with the monoglycopeptide 3

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000139	cellular_component	Golgi membrane
A	0004653	molecular_function	polypeptide N-acetylgalactosaminyltransferase activity
A	0005515	molecular_function	protein binding
A	0005794	cellular_component	Golgi apparatus
A	0006486	biological_process	protein glycosylation
A	0006493	biological_process	protein O-linked glycosylation
A	0016020	cellular_component	membrane
A	0016266	biological_process	core O-glycan biosynthetic process
A	0016740	molecular_function	transferase activity
A	0016757	molecular_function	glycosyltransferase activity
A	0018242	biological_process	protein O-linked glycosylation via serine
A	0018243	biological_process	protein O-linked glycosylation via threonine
A	0030145	molecular_function	manganese ion binding
A	0030246	molecular_function	carbohydrate binding
A	0046872	molecular_function	metal ion binding
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0070062	cellular_component	extracellular exosome
B	0000139	cellular_component	Golgi membrane
B	0004653	molecular_function	polypeptide N-acetylgalactosaminyltransferase activity
B	0005515	molecular_function	protein binding
B	0005794	cellular_component	Golgi apparatus
B	0006486	biological_process	protein glycosylation
B	0006493	biological_process	protein O-linked glycosylation
B	0016020	cellular_component	membrane
B	0016266	biological_process	core O-glycan biosynthetic process
B	0016740	molecular_function	transferase activity
B	0016757	molecular_function	glycosyltransferase activity
B	0018242	biological_process	protein O-linked glycosylation via serine
B	0018243	biological_process	protein O-linked glycosylation via threonine
B	0030145	molecular_function	manganese ion binding
B	0030246	molecular_function	carbohydrate binding
B	0046872	molecular_function	metal ion binding
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0070062	cellular_component	extracellular exosome

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	266
Details	Domain: {"description":"Ricin B-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00174","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	218
Details	Region: {"description":"Catalytic subdomain A"}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	124
Details	Region: {"description":"Catalytic subdomain B"}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q10471","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	6
Details	Site: {"description":"Interaction with glycopeptide substrate","evidences":[{"source":"PubMed","id":"29208955","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI6
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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