5F86
Crystal structure of Drosophila Poglut1 (Rumi) complexed with its substrate protein (EGF repeat)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0006486 | biological_process | 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 | 0018242 | biological_process | protein O-linked glycosylation via serine |
| 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 |
| B | 0005509 | molecular_function | calcium ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | ARG125 |
| A | ASP151 |
| A | ALA295 |
| A | SER296 |
| A | PHE297 |
| A | SO4502 |
| A | HOH637 |
| A | HOH658 |
| B | SER53 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 A 502 |
| Chain | Residue |
| A | THR233 |
| A | ARG237 |
| A | SER296 |
| A | ARG298 |
| A | GOL501 |
| A | HOH637 |
| A | HOH649 |
| A | HOH688 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 A 503 |
| Chain | Residue |
| A | HIS196 |
| A | MET206 |
| A | LYS209 |
| A | SER277 |
| A | PHE278 |
| A | GLU279 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 504 |
| Chain | Residue |
| A | LYS49 |
| A | ASP314 |
| A | LYS334 |
| A | SER335 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | binding site for residue SO4 A 505 |
| Chain | Residue |
| A | ARG229 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 A 506 |
| Chain | Residue |
| A | SER239 |
| A | SER338 |
| A | SER338 |
| A | GLN339 |
| A | GLN339 |
| A | HOH626 |
| A | HOH626 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 507 |
| Chain | Residue |
| A | ARG372 |
| A | MET373 |
| A | LYS374 |
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 | BINDING: BINDING => ECO:0000269|PubMed:7606779, ECO:0007744|PDB:1EDM |
| Chain | Residue | Details |
| B | ASP47 | |
| B | GLY48 | |
| B | GLN50 | |
| B | ASP64 | |
| B | ASP65 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: (3R)-3-hydroxyaspartate => ECO:0000269|PubMed:6688526 |
| Chain | Residue | Details |
| B | ASP64 | |
| A | ARG237 | |
| A | VAL276 | |
| A | ALA294 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|Ref.28 |
| Chain | Residue | Details |
| B | SER68 | |
| A | ARG232 | |
| A | GLN259 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (Glc...) serine => ECO:0000269|PubMed:2129367, ECO:0000269|PubMed:2511201, ECO:0000269|PubMed:25456591 |
| Chain | Residue | Details |
| B | SER53 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | CARBOHYD: O-linked (Fuc...) serine => ECO:0000269|PubMed:1517205, ECO:0000269|PubMed:25456591 |
| Chain | Residue | Details |
| B | SER61 |
