1Y4J
Crystal structure of the paralogue of the human formylglycine generating enzyme
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004857 | molecular_function | enzyme inhibitor activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005788 | cellular_component | endoplasmic reticulum lumen |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0043687 | biological_process | post-translational protein modification |
| A | 0046479 | biological_process | glycosphingolipid catabolic process |
| B | 0004857 | molecular_function | enzyme inhibitor activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005788 | cellular_component | endoplasmic reticulum lumen |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0043687 | biological_process | post-translational protein modification |
| B | 0046479 | biological_process | glycosphingolipid catabolic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Compositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15687489","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"15687489","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
