7OPN
Human Aldehyde Oxidase SNP R1231H in complex with Raloxifene
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004031 | molecular_function | aldehyde oxidase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006805 | biological_process | xenobiotic metabolic process |
| A | 0015630 | cellular_component | microtubule cytoskeleton |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016604 | cellular_component | nuclear body |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0045171 | cellular_component | intercellular bridge |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0051287 | molecular_function | NAD binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0071949 | molecular_function | FAD binding |
| B | 0004031 | molecular_function | aldehyde oxidase activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006629 | biological_process | lipid metabolic process |
| B | 0006805 | biological_process | xenobiotic metabolic process |
| B | 0015630 | cellular_component | microtubule cytoskeleton |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016604 | cellular_component | nuclear body |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0043546 | molecular_function | molybdopterin cofactor binding |
| B | 0045171 | cellular_component | intercellular bridge |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0051287 | molecular_function | NAD binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0070062 | cellular_component | extracellular exosome |
| B | 0071949 | molecular_function | FAD binding |
Functional Information from PROSITE/UniProt
| site_id | PS00197 |
| Number of Residues | 9 |
| Details | 2FE2S_FER_1 2Fe-2S ferredoxin-type iron-sulfur binding region signature. CGGGGCGAC |
| Chain | Residue | Details |
| A | CYS44-CYS52 |
| site_id | PS00559 |
| Number of Residues | 36 |
| Details | MOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. AFggKvlktgiiaavta..FaanKHgraVrCvlERgeD |
| Chain | Residue | Details |
| A | ALA806-ASP841 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 174 |
| Details | Domain: {"description":"2Fe-2S ferredoxin-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00465","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 370 |
| Details | Domain: {"description":"FAD-binding PCMH-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00718","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor; for azaheterocycle hydroxylase activity","evidences":[{"source":"UniProtKB","id":"O54754","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UHW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 46 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26842593","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UHW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UHX","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5EPG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UHW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UHX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26842593","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5EPG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26322824","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4UHX","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
