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4F9U

Structure of glycosylated glutaminyl cyclase from Drosophila melanogaster

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008270molecular_functionzinc ion binding
A0016603molecular_functionglutaminyl-peptide cyclotransferase activity
A0016746molecular_functionacyltransferase activity
A0046872molecular_functionmetal ion binding
B0005576cellular_componentextracellular region
B0008270molecular_functionzinc ion binding
B0016603molecular_functionglutaminyl-peptide cyclotransferase activity
B0016746molecular_functionacyltransferase activity
B0046872molecular_functionmetal ion binding
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q16769
ChainResidueDetails
AGLU170
AASP218
BGLU170
BASP218

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:22897232, ECO:0007744|PDB:4F9V
ChainResidueDetails
AARG85
AGLU91
BARG85
BGLU91

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22897232, ECO:0000269|PubMed:23545638, ECO:0007744|PDB:4F9U, ECO:0007744|PDB:4F9V, ECO:0007744|PDB:4FWU
ChainResidueDetails
AASP131
AGLU171
AHIS297
BASP131
BGLU171
BHIS297

site_idSWS_FT_FI4
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:22897232, ECO:0007744|PDB:4F9U
ChainResidueDetails
AGLN151
AARG155
ALEU306
BGLN151
BARG155
BLEU306

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:22897232, ECO:0000269|PubMed:23545638, ECO:0000312|PDB:4FWU, ECO:0007744|PDB:4F9U, ECO:0007744|PDB:4F9V
ChainResidueDetails
AASN42
BASN42

site_idSWS_FT_FI6
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255|PROSITE-ProRule:PRU00498
ChainResidueDetails
AASN156
BASN156

224004

PDB entries from 2024-08-21

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