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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5F86

Crystal structure of Drosophila Poglut1 (Rumi) complexed with its substrate protein (EGF repeat)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005783cellular_componentendoplasmic reticulum
A0005788cellular_componentendoplasmic reticulum lumen
A0006486biological_processprotein glycosylation
A0006493biological_processprotein O-linked glycosylation
A0007219biological_processNotch signaling pathway
A0012505cellular_componentendomembrane system
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0018242biological_processprotein O-linked glycosylation via serine
A0035251molecular_functionUDP-glucosyltransferase activity
A0035252molecular_functionUDP-xylosyltransferase activity
A0042052biological_processrhabdomere development
A0045165biological_processcell fate commitment
A0045746biological_processnegative regulation of Notch signaling pathway
A0045747biological_processpositive regulation of Notch signaling pathway
A0046527molecular_functionglucosyltransferase activity
A0060537biological_processmuscle tissue development
A0140561molecular_functionEGF-domain serine glucosyltransferase activity
A0140562molecular_functionEGF-domain serine xylosyltransferase activity
B0005509molecular_functioncalcium ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue GOL A 501
ChainResidue
AARG125
AASP151
AALA295
ASER296
APHE297
ASO4502
AHOH637
AHOH658
BSER53
site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 A 502
ChainResidue
ATHR233
AARG237
ASER296
AARG298
AGOL501
AHOH637
AHOH649
AHOH688
site_idAC3
Number of Residues6
Detailsbinding site for residue SO4 A 503
ChainResidue
AHIS196
AMET206
ALYS209
ASER277
APHE278
AGLU279
site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 A 504
ChainResidue
ALYS49
AASP314
ALYS334
ASER335
site_idAC5
Number of Residues1
Detailsbinding site for residue SO4 A 505
ChainResidue
AARG229
site_idAC6
Number of Residues7
Detailsbinding site for residue SO4 A 506
ChainResidue
ASER239
ASER338
ASER338
AGLN339
AGLN339
AHOH626
AHOH626
site_idAC7
Number of Residues3
Detailsbinding site for residue SO4 A 507
ChainResidue
AARG372
AMET373
ALYS374
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC
ChainResidueDetails
BCYS62-CYS73
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CwCpfGfeGKnC
ChainResidueDetails
BCYS71-CYS82
site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CwCpfGFegkn....C
ChainResidueDetails
BCYS71-CYS82
site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC
ChainResidueDetails
BASP47-CYS71
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsRegion: {"description":"Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates","evidences":[{"source":"PubMed","id":"27428513","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"27428513","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27428513","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5F84","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F85","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5F87","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsSite: {"description":"Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates","evidences":[{"source":"PubMed","id":"27428513","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7606779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EDM","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6688526","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"book","publicationDate":"1996","firstPage":"50","lastPage":"50","publisher":"Annecy","bookName":"Proceedings of XIth international conference on methods in protein structure analysis","title":"Partial phosphorylation of serine-68 in EGF-1 of human factor IX.","authors":["Harris R.J.","Papac D.I.","Truong L.","Smith K.J."]}}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Glc...) serine","featureId":"CAR_000009","evidences":[{"source":"PubMed","id":"2129367","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2511201","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25456591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Fuc...) serine","featureId":"CAR_000010","evidences":[{"source":"PubMed","id":"1517205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25456591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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