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3PBE

Crystal structure of the mutant W207F of human secretory glutaminyl cyclase

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
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
A0035580cellular_componentspecific granule lumen
A0036211biological_processprotein modification process
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A1904724cellular_componenttertiary granule lumen
A1904813cellular_componentficolin-1-rich granule lumen
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0008270molecular_functionzinc ion binding
B0016603molecular_functionglutaminyl-peptide cyclotransferase activity
B0016740molecular_functiontransferase activity
B0016746molecular_functionacyltransferase activity
B0017186biological_processpeptidyl-pyroglutamic acid biosynthetic process, using glutaminyl-peptide cyclotransferase
B0035580cellular_componentspecific granule lumen
B0036211biological_processprotein modification process
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B1904724cellular_componenttertiary granule lumen
B1904813cellular_componentficolin-1-rich granule lumen
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 391
ChainResidue
AASP159
AGLU202
AHIS330
AHOH861

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ZN B 392
ChainResidue
BASP159
BGLU202
BHIS330
BHOH867

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 395
ChainResidue
ALEU205
AHIS206
APHE207
AASN263
ATRP329
AHIS330
AHOH574
AHOH703
AHOH893
ALYS144

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 B 396
ChainResidue
BLYS40
BLYS144
BLEU205
BHIS206
BPHE207
BHOH603
BHOH604
BHOH725
BHOH836
BHOH846

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"18072935","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"16135565","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18072935","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21288892","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21671571","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AFM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2AFZ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZED","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2ZEP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PBB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3PBE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3SI0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YU9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4YWY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"21671571","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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

246031

PDB entries from 2025-12-10

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