3SI2

Structure of glycosylated murine glutaminyl cyclase in presence of the inhibitor PQ50 (PDBD150)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005576	cellular_component	extracellular region
A	0008270	molecular_function	zinc ion binding
A	0016603	molecular_function	glutaminyl-peptide cyclotransferase activity
A	0016746	molecular_function	acyltransferase activity
A	0017186	biological_process	peptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
A	0046872	molecular_function	metal ion binding

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q16769

Chain	Residue	Details
A	GLU202
A	ASP249

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site_id	SWS_FT_FI2
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:21671571, ECO:0007744|PDB:3SI1, ECO:0007744|PDB:3SI2

Chain	Residue	Details
A	ASP160
A	GLU203
A	HIS331

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site_id	SWS_FT_FI3
Number of Residues	1
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:21671571, ECO:0007744|PDB:3SI1, ECO:0007744|PDB:3SI2

Chain	Residue	Details
A	ASN50

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