8SNN
Structure of mature human ADAM17/iRhom2 sheddase complex, conformation 1
Functional Information from GO Data
Chain | GOid | namespace | contents |
B | 0002862 | biological_process | negative regulation of inflammatory response to antigenic stimulus |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005783 | cellular_component | endoplasmic reticulum |
B | 0005789 | cellular_component | endoplasmic reticulum membrane |
B | 0005796 | cellular_component | Golgi lumen |
B | 0005886 | cellular_component | plasma membrane |
B | 0015031 | biological_process | protein transport |
B | 0019838 | molecular_function | growth factor binding |
B | 0042058 | biological_process | regulation of epidermal growth factor receptor signaling pathway |
B | 0050708 | biological_process | regulation of protein secretion |
B | 0050709 | biological_process | negative regulation of protein secretion |
B | 0072659 | biological_process | protein localization to plasma membrane |
B | 0140318 | molecular_function | protein transporter activity |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VTTHELGHNF |
Chain | Residue | Details |
A | VAL402-PHE411 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 435 |
Details | TOPO_DOM: Cytoplasmic => ECO:0000255 |
Chain | Residue | Details |
B | MET1-LEU409 | |
B | PHE682-ALA692 | |
B | PRO737-GLY747 | |
B | TYR795-PRO802 |
site_id | SWS_FT_FI2 |
Number of Residues | 140 |
Details | TRANSMEM: Helical => ECO:0000255 |
Chain | Residue | Details |
B | VAL410-VAL430 | |
B | TRP661-ILE681 | |
B | GLY693-LEU713 | |
B | PRO716-LEU736 | |
B | PHE748-ASP768 | |
B | ALA774-LEU794 | |
B | TRP803-ASP823 |
site_id | SWS_FT_FI3 |
Number of Residues | 234 |
Details | TOPO_DOM: Lumenal => ECO:0000255 |
Chain | Residue | Details |
B | GLY431-GLY660 | |
B | GLU714-ARG715 | |
B | LYS769-ARG773 |
site_id | SWS_FT_FI4 |
Number of Residues | 3 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | ARG90 | |
B | ALA325 | |
B | VAL328 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
B | ARG113 | |
A | HIS409 | |
A | HIS415 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q80WQ6 |
Chain | Residue | Details |
B | HIS117 | |
B | ARG323 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
Chain | Residue | Details |
A | THR761 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Z1K9 |
Chain | Residue | Details |
A | SER767 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER791 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:12621058 |
Chain | Residue | Details |
A | SER819 |
site_id | SWS_FT_FI11 |
Number of Residues | 6 |
Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
Chain | Residue | Details |
A | ASN264 | |
A | ASN452 | |
A | ASN498 | |
A | ASN539 | |
A | ASN551 | |
A | ASN594 |