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4MHY

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

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008270molecular_functionzinc ion binding
A0016603molecular_functionglutaminyl-peptide cyclotransferase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0017186biological_processpeptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 400
ChainResidue
AASP144
AGLU184
AHIS322
APBD401

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PBD A 401
ChainResidue
AGLU296
APHE317
ATRP321
AHIS322
AZN400
AHOH743
AHOH777
AASP144
AGLU183
AGLU184
ATRP189
AASP238

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q16769","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"24598748","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"24598748","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4MHN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4MHY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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