4MHY

Crystal structure of a glutaminyl cyclase from Ixodes scapularis in complex with PBD150

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 PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 400

Chain	Residue
A	ASP144
A	GLU184
A	HIS322
A	PBD401

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site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PBD A 401

Chain	Residue
A	GLU296
A	PHE317
A	TRP321
A	HIS322
A	ZN400
A	HOH743
A	HOH777
A	ASP144
A	GLU183
A	GLU184
A	TRP189
A	ASP238

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q16769

Chain	Residue	Details
A	GLU183

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site_id	SWS_FT_FI2
Number of Residues	1
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:24598748

Chain	Residue	Details
A	ASP238

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site_id	SWS_FT_FI3
Number of Residues	3
Details	BINDING: BINDING => ECO:0000269|PubMed:24598748, ECO:0007744|PDB:4MHN, ECO:0007744|PDB:4MHY

Chain	Residue	Details
A	ASP144
A	GLU184
A	HIS322

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site_id	SWS_FT_FI4
Number of Residues	2
Details	CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498

Chain	Residue	Details
A	ASN57
A	ASN288

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