7D3E
Cryo-EM structure of human DUOX1-DUOXA1 in low-calcium state
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0020037 | molecular_function | heme binding |
| B | 0005515 | molecular_function | protein binding |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008104 | biological_process | intracellular protein localization |
| B | 0010729 | biological_process | positive regulation of hydrogen peroxide biosynthetic process |
| B | 0015031 | biological_process | protein transport |
| B | 0016020 | cellular_component | membrane |
| B | 0016324 | cellular_component | apical plasma membrane |
| B | 0050665 | biological_process | hydrogen peroxide biosynthetic process |
| B | 0072659 | biological_process | protein localization to plasma membrane |
| B | 2000609 | biological_process | regulation of thyroid hormone generation |
| C | 0004601 | molecular_function | peroxidase activity |
| C | 0005509 | molecular_function | calcium ion binding |
| C | 0006979 | biological_process | response to oxidative stress |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0020037 | molecular_function | heme binding |
| D | 0005515 | molecular_function | protein binding |
| D | 0005789 | cellular_component | endoplasmic reticulum membrane |
| D | 0005886 | cellular_component | plasma membrane |
| D | 0008104 | biological_process | intracellular protein localization |
| D | 0010729 | biological_process | positive regulation of hydrogen peroxide biosynthetic process |
| D | 0015031 | biological_process | protein transport |
| D | 0016020 | cellular_component | membrane |
| D | 0016324 | cellular_component | apical plasma membrane |
| D | 0050665 | biological_process | hydrogen peroxide biosynthetic process |
| D | 0072659 | biological_process | protein localization to plasma membrane |
| D | 2000609 | biological_process | regulation of thyroid hormone generation |
Functional Information from PROSITE/UniProt
| site_id | PS00018 |
| Number of Residues | 13 |
| Details | EF_HAND_1 EF-hand calcium-binding domain. DKDGNGYLSfrEF |
| Chain | Residue | Details |
| A | ASP828-PHE840 | |
| A | ASP864-PHE876 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1480 |
| Details | Topological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"33420071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7D3F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 522 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33420071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7D3F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 80 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"33420071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7D3F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 280 |
| Details | Domain: {"description":"Ferric oxidoreductase","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1134 |
| Details | Region: {"description":"Peroxidase-like"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 44 |
| Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"A2AQ92","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"33420071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7D3F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33420071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7D3F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 38 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33420071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7D3E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7D3F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"33420071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7D3E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7D3F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"33420071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7D3E","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 12 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"33420071","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7D3E","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7D3F","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
