9UB7
Structure of glycosylphosphatidylinositol transamidase,state 1
This is a non-PDB format compatible entry.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003674 | molecular_function | molecular_function |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006506 | biological_process | GPI anchor biosynthetic process |
| A | 0016255 | biological_process | attachment of GPI anchor to protein |
| A | 0031505 | biological_process | fungal-type cell wall organization |
| A | 0042765 | cellular_component | GPI-anchor transamidase complex |
| B | 0003674 | molecular_function | molecular_function |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0006506 | biological_process | GPI anchor biosynthetic process |
| B | 0016255 | biological_process | attachment of GPI anchor to protein |
| B | 0031505 | biological_process | fungal-type cell wall organization |
| B | 0042765 | cellular_component | GPI-anchor transamidase complex |
| D | 0003674 | molecular_function | molecular_function |
| D | 0005515 | molecular_function | protein binding |
| D | 0005637 | cellular_component | nuclear inner membrane |
| D | 0005783 | cellular_component | endoplasmic reticulum |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0006506 | biological_process | GPI anchor biosynthetic process |
| D | 0016020 | cellular_component | membrane |
| D | 0016255 | biological_process | attachment of GPI anchor to protein |
| D | 0031505 | biological_process | fungal-type cell wall organization |
| D | 0042765 | cellular_component | GPI-anchor transamidase complex |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 340 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 428 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 195 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | Region: {"description":"May be involved in recognition of long-chain fatty acids in GPI","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"11598210","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
