5F84
Crystal structure of Drosophila Poglut1 (Rumi) complexed with its glycoprotein product (glucosylated EGF repeat) and UDP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0006486 | biological_process | obsolete protein glycosylation |
| A | 0006493 | biological_process | protein O-linked glycosylation |
| A | 0007219 | biological_process | Notch signaling pathway |
| A | 0012505 | cellular_component | endomembrane system |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0035251 | molecular_function | UDP-glucosyltransferase activity |
| A | 0035252 | molecular_function | UDP-xylosyltransferase activity |
| A | 0042052 | biological_process | rhabdomere development |
| A | 0045165 | biological_process | cell fate commitment |
| A | 0045746 | biological_process | negative regulation of Notch signaling pathway |
| A | 0045747 | biological_process | positive regulation of Notch signaling pathway |
| A | 0046527 | molecular_function | glucosyltransferase activity |
| A | 0060537 | biological_process | muscle tissue development |
| A | 0140561 | molecular_function | EGF-domain serine glucosyltransferase activity |
| A | 0140562 | molecular_function | EGF-domain serine xylosyltransferase activity |
| A | 0180059 | biological_process | protein O-linked glycosylation via glucose |
| B | 0005509 | molecular_function | calcium ion binding |
Functional Information from PROSITE/UniProt
| site_id | PS00010 |
| Number of Residues | 12 |
| Details | ASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDdinsYeCwC |
| Chain | Residue | Details |
| B | CYS62-CYS73 |
| site_id | PS00022 |
| Number of Residues | 12 |
| Details | EGF_1 EGF-like domain signature 1. CwCpfGfeGKnC |
| Chain | Residue | Details |
| B | CYS71-CYS82 |
| site_id | PS01186 |
| Number of Residues | 12 |
| Details | EGF_2 EGF-like domain signature 2. CwCpfGFegkn....C |
| Chain | Residue | Details |
| B | CYS71-CYS82 |
| site_id | PS01187 |
| Number of Residues | 25 |
| Details | EGF_CA Calcium-binding EGF-like domain signature. DgDQCesnp..........Clnggs..CkDdinsYeC |
| Chain | Residue | Details |
| B | ASP47-CYS71 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 5 |
| Details | Region: {"description":"Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates","evidences":[{"source":"PubMed","id":"27428513","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"27428513","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | Binding 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Site: {"description":"Interaction with the consensus sequence C-X-S-X-[PA]-C in peptide substrates","evidences":[{"source":"PubMed","id":"27428513","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7606779","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EDM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6688526","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified 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."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"O-linked (Fuc...) serine","featureId":"CAR_000010","evidences":[{"source":"PubMed","id":"1517205","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25456591","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
