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 | 0001933 | biological_process | negative regulation of protein phosphorylation |
A | 0001937 | biological_process | negative regulation of endothelial cell proliferation |
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 | 0010629 | biological_process | negative regulation of gene expression |
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 | 0043605 | biological_process | amide catabolic process |
A | 0045602 | biological_process | negative regulation of endothelial cell differentiation |
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 | 0051898 | biological_process | negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction |
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 |
A | 1900745 | biological_process | positive regulation of p38MAPK cascade |
A | 1900747 | biological_process | negative regulation of vascular endothelial growth factor signaling pathway |
A | 2000379 | biological_process | positive regulation of reactive oxygen species metabolic process |
A | 2001213 | biological_process | negative regulation of vasculogenesis |
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 | 1 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | PRO1262 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17301076, ECO:0007744|PDB:2E3T |
Chain | Residue | Details |
A | GLY44 | |
A | GLY49 | |
A | THR52 | |
A | LEU74 | |
A | GLY113 | |
A | THR116 | |
A | ARG148 | |
A | THR150 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15878860, ECO:0000269|PubMed:17301076 |
Chain | Residue | Details |
A | VAL257 | |
A | ILE347 | |
A | LEU360 | |
A | LEU404 |
site_id | SWS_FT_FI4 |
Number of Residues | 7 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | ALA337 | |
A | GLN422 | |
A | ASN768 | |
A | GLY799 | |
A | GLY913 | |
A | GLY915 | |
A | SER1080 |
site_id | SWS_FT_FI5 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | THR803 | |
A | ALA881 | |
A | LEU1011 |
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 |