6Q6Q
Human aldehyde oxidase SNP G1269R
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 | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue FES A 3001 |
| Chain | Residue |
| A | GLN113 |
| A | CYS114 |
| A | GLY115 |
| A | CYS117 |
| A | CYS149 |
| A | ARG150 |
| A | CYS151 |
| A | MET753 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue FES A 3002 |
| Chain | Residue |
| A | CYS44 |
| A | GLY45 |
| A | GLY47 |
| A | GLY48 |
| A | CYS49 |
| A | GLY50 |
| A | CYS52 |
| A | CYS74 |
| A | GLY43 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | binding site for residue FAD A 3003 |
| Chain | Residue |
| A | GLY46 |
| A | GLY47 |
| A | PRO263 |
| A | VAL264 |
| A | ILE265 |
| A | MET266 |
| A | GLY267 |
| A | ASN268 |
| A | THR269 |
| A | SER270 |
| A | VAL271 |
| A | LEU344 |
| A | ALA345 |
| A | ALA353 |
| A | SER354 |
| A | GLY357 |
| A | HIS358 |
| A | ILE360 |
| A | SER361 |
| A | HIS363 |
| A | ASP365 |
| A | SER366 |
| A | ASP367 |
| A | LEU411 |
| A | LEU438 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue MLI A 3004 |
| Chain | Residue |
| A | CYS44 |
| A | LEU148 |
| A | ARG433 |
| A | TYR1236 |
| A | LYS1237 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue MLI A 3005 |
| Chain | Residue |
| A | ARG32 |
| A | LYS33 |
| A | THR38 |
| A | ASP601 |
| A | MET603 |
| A | LEU605 |
| A | HOH3103 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue MLI A 3006 |
| Chain | Residue |
| A | THR616 |
| A | ALA690 |
| A | LYS691 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue MLI A 3007 |
| Chain | Residue |
| A | PHE807 |
| A | GLY808 |
| A | ALA919 |
| A | PHE920 |
| A | GLY1087 |
| A | GLU1270 |
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 | 87 |
| 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 | 185 |
| 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 | 1 |
| 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 | 1 |
| 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 | 23 |
| 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 | 2 |
| 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 | 1 |
| 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 | 1 |
| 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 | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
