1WYG
Crystal Structure of a Rat Xanthine Dehydrogenase Triple Mutant (C535A, C992R and C1324S)
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000255 | biological_process | allantoin metabolic process |
| A | 0004854 | molecular_function | xanthine dehydrogenase activity |
| A | 0004855 | molecular_function | xanthine oxidase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005615 | cellular_component | extracellular space |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005777 | cellular_component | peroxisome |
| A | 0005829 | cellular_component | cytosol |
| A | 0006147 | biological_process | guanine catabolic process |
| A | 0006148 | biological_process | inosine catabolic process |
| A | 0006149 | biological_process | deoxyinosine catabolic process |
| A | 0006154 | biological_process | adenosine catabolic process |
| A | 0006157 | biological_process | deoxyadenosine catabolic process |
| A | 0006161 | biological_process | deoxyguanosine catabolic process |
| A | 0006196 | biological_process | AMP catabolic process |
| A | 0006204 | biological_process | IMP catabolic process |
| A | 0007595 | biological_process | lactation |
| A | 0009114 | biological_process | hypoxanthine catabolic process |
| A | 0009115 | biological_process | xanthine catabolic process |
| A | 0010044 | biological_process | response to aluminum ion |
| A | 0016226 | biological_process | iron-sulfur cluster assembly |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016529 | cellular_component | sarcoplasmic reticulum |
| A | 0030856 | biological_process | regulation of epithelial cell differentiation |
| A | 0032496 | biological_process | response to lipopolysaccharide |
| A | 0034465 | biological_process | response to carbon monoxide |
| A | 0042542 | biological_process | response to hydrogen peroxide |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0043546 | molecular_function | molybdopterin cofactor binding |
| A | 0046038 | biological_process | GMP catabolic process |
| A | 0046055 | biological_process | dGMP catabolic process |
| A | 0046059 | biological_process | dAMP catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0050421 | molecular_function | nitrite reductase (NO-forming) activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| A | 0070674 | molecular_function | hypoxanthine dehydrogenase activity |
| A | 0070675 | molecular_function | hypoxanthine oxidase activity |
| A | 0071347 | biological_process | cellular response to interleukin-1 |
| A | 0071356 | biological_process | cellular response to tumor necrosis factor |
| A | 0071949 | molecular_function | FAD binding |
| A | 0097184 | biological_process | response to azide |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2001 |
| Chain | Residue |
| A | GLN1040 |
| A | SER1080 |
| A | SER1082 |
| A | ALA1083 |
| A | ACY3001 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2002 |
| Chain | Residue |
| A | PRO937 |
| A | ALA938 |
| A | LYS981 |
| A | ASP1276 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE PO4 A 2003 |
| Chain | Residue |
| A | THR611 |
| A | ARG612 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE CA A 4001 |
| Chain | Residue |
| A | GLY867 |
| A | THR870 |
| A | GLU871 |
| A | ASP872 |
| A | SER874 |
| A | SER907 |
| A | ASN908 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 4002 |
| Chain | Residue |
| A | GLN111 |
| A | CYS112 |
| A | CYS115 |
| A | CYS147 |
| A | ARG148 |
| A | CYS149 |
| A | LEU744 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE FES A 4003 |
| Chain | Residue |
| A | GLY42 |
| A | CYS43 |
| A | GLY44 |
| A | GLY46 |
| A | GLY47 |
| A | CYS48 |
| A | GLY49 |
| A | CYS51 |
| A | ASN71 |
| A | CYS73 |
| site_id | AC7 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD A 4004 |
| Chain | Residue |
| A | GLU45 |
| A | GLY46 |
| A | LYS255 |
| A | LEU256 |
| A | VAL257 |
| A | VAL258 |
| A | GLY259 |
| A | ASN260 |
| A | THR261 |
| A | GLU262 |
| A | ILE263 |
| A | ALA300 |
| A | TRP335 |
| A | PHE336 |
| A | ALA337 |
| A | VAL341 |
| A | ALA345 |
| A | SER346 |
| A | GLY349 |
| A | ASN350 |
| A | ILE352 |
| A | THR353 |
| A | SER358 |
| A | ASP359 |
| A | ILE402 |
| A | LEU403 |
| A | LYS421 |
| A | ASP428 |
| A | ASP429 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SAL A 4005 |
| Chain | Residue |
| A | GLU802 |
| A | ARG880 |
| A | PHE914 |
| A | PHE1009 |
| A | THR1010 |
| A | ALA1078 |
| A | ALA1079 |
| A | GLU1261 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ACY A 3001 |
| Chain | Residue |
| A | ALA1078 |
| A | ALA1079 |
| A | SER1080 |
| A | PO42001 |
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. CGEGGCGAC |
| Chain | Residue | Details |
| A | CYS43-CYS51 |
| site_id | PS00559 |
| Number of Residues | 36 |
| Details | MOLYBDOPTERIN_EUK Eukaryotic molybdopterin oxidoreductases signature. GFggKetrstvvstala..LaahKTgrpVrCmlDRdeD |
| Chain | Residue | Details |
| A | GLY797-ASP832 |
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"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17301076","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2E3T","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15878860","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17301076","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 3 |
| Details | Binding site: {} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| A | GLU1261 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| A | ARG912 | |
| A | GLN767 |
