1FO4
CRYSTAL STRUCTURE OF XANTHINE DEHYDROGENASE ISOLATED FROM BOVINE MILK
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0002197 | cellular_component | xanthine dehydrogenase complex |
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 | 0009115 | biological_process | xanthine catabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0030151 | molecular_function | molybdenum ion 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 | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
A | 0071949 | molecular_function | FAD binding |
B | 0002197 | cellular_component | xanthine dehydrogenase complex |
B | 0004854 | molecular_function | xanthine dehydrogenase activity |
B | 0004855 | molecular_function | xanthine oxidase activity |
B | 0005506 | molecular_function | iron ion binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005615 | cellular_component | extracellular space |
B | 0005737 | cellular_component | cytoplasm |
B | 0005777 | cellular_component | peroxisome |
B | 0009115 | biological_process | xanthine catabolic process |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0030151 | molecular_function | molybdenum ion binding |
B | 0042803 | molecular_function | protein homodimerization activity |
B | 0043546 | molecular_function | molybdopterin cofactor binding |
B | 0046872 | molecular_function | metal ion binding |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
B | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 4009 |
Chain | Residue |
A | ALA867 |
A | SER870 |
A | ARG871 |
A | SER874 |
A | SER907 |
A | ASN908 |
site_id | AC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE CA B 4019 |
Chain | Residue |
B | ASP872 |
B | SER874 |
B | SER907 |
B | ASN908 |
B | ALA867 |
B | SER870 |
B | ARG871 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES A 3001 |
Chain | Residue |
A | GLN112 |
A | CYS113 |
A | GLY114 |
A | CYS116 |
A | CYS148 |
A | ARG149 |
A | CYS150 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE FES A 3002 |
Chain | Residue |
A | GLY42 |
A | CYS43 |
A | GLY44 |
A | GLY46 |
A | GLY47 |
A | CYS48 |
A | GLY49 |
A | CYS51 |
A | ASN71 |
A | CYS73 |
site_id | AC5 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE MTE A 3003 |
Chain | Residue |
A | GLN112 |
A | CYS150 |
A | GLY796 |
A | GLY797 |
A | PHE798 |
A | ARG912 |
A | MET1038 |
A | GLY1039 |
A | GLN1040 |
A | ALA1078 |
A | ALA1079 |
A | SER1080 |
A | VAL1081 |
A | SER1082 |
A | GLN1194 |
A | GLU1261 |
A | MOS3004 |
A | HOH4182 |
A | HOH4375 |
A | HOH4575 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MOS A 3004 |
Chain | Residue |
A | GLN767 |
A | GLY799 |
A | GLU802 |
A | PHE911 |
A | ARG912 |
A | ALA1078 |
A | ALA1079 |
A | GLU1261 |
A | MTE3003 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE SAL A 3005 |
Chain | Residue |
A | GLU802 |
A | ARG880 |
A | PHE914 |
A | PHE1009 |
A | THR1010 |
A | VAL1011 |
A | ALA1079 |
A | HOH4231 |
site_id | AC8 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD A 3006 |
Chain | Residue |
A | HOH4301 |
A | HOH4510 |
A | GLU45 |
A | GLY46 |
A | GLY47 |
A | LEU74 |
A | LYS256 |
A | LEU257 |
A | VAL258 |
A | VAL259 |
A | GLY260 |
A | ASN261 |
A | THR262 |
A | GLU263 |
A | ILE264 |
A | ALA301 |
A | PHE337 |
A | ALA338 |
A | VAL342 |
A | ALA346 |
A | SER347 |
A | GLY350 |
A | ASN351 |
A | ILE353 |
A | THR354 |
A | SER359 |
A | ASP360 |
A | ILE403 |
A | LEU404 |
A | LYS422 |
A | ASP429 |
A | HOH4132 |
A | HOH4143 |
A | HOH4187 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FES B 4001 |
Chain | Residue |
B | GLN112 |
B | CYS113 |
B | GLY114 |
B | CYS116 |
B | CYS148 |
B | ARG149 |
B | CYS150 |
site_id | BC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE FES B 4002 |
Chain | Residue |
B | GLY42 |
B | CYS43 |
B | GLY44 |
B | GLY46 |
B | GLY47 |
B | CYS48 |
B | GLY49 |
B | CYS51 |
B | ASN71 |
B | CYS73 |
site_id | BC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE MTE B 4003 |
Chain | Residue |
B | GLN112 |
B | CYS150 |
B | GLY796 |
B | GLY797 |
B | PHE798 |
B | ARG912 |
B | MET1038 |
B | GLY1039 |
B | GLN1040 |
B | ALA1078 |
B | ALA1079 |
B | SER1080 |
B | VAL1081 |
B | SER1082 |
B | GLN1194 |
B | GLU1261 |
B | MOS4004 |
B | HOH4205 |
B | HOH4392 |
B | HOH4583 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE MOS B 4004 |
Chain | Residue |
B | GLN767 |
B | PHE798 |
B | GLY799 |
B | GLU802 |
B | PHE911 |
B | ARG912 |
B | ALA1078 |
B | ALA1079 |
B | GLU1261 |
B | MTE4003 |
site_id | BC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE SAL B 4005 |
Chain | Residue |
B | GLU802 |
B | ARG880 |
B | PHE914 |
B | PHE1009 |
B | THR1010 |
B | HOH4254 |
site_id | BC5 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD B 4006 |
Chain | Residue |
B | GLU45 |
B | GLY46 |
B | GLY47 |
B | LEU74 |
B | LYS256 |
B | LEU257 |
B | VAL258 |
B | VAL259 |
B | GLY260 |
B | ASN261 |
B | THR262 |
B | GLU263 |
B | ILE264 |
B | ALA301 |
B | PHE337 |
B | ALA338 |
B | VAL342 |
B | ALA346 |
B | SER347 |
B | GLY350 |
B | ASN351 |
B | ILE353 |
B | SER359 |
B | ASP360 |
B | ILE403 |
B | LEU404 |
B | LYS422 |
B | ASP429 |
B | ASP430 |
B | HOH4157 |
B | HOH4167 |
B | HOH4210 |
B | HOH4322 |
site_id | BC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 3007 |
Chain | Residue |
A | ARG839 |
A | HIS840 |
A | ILE877 |
A | THR909 |
A | ALA910 |
A | PHE911 |
A | GLY913 |
A | PHE914 |
A | GLY915 |
A | GLN918 |
site_id | BC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 3008 |
Chain | Residue |
A | GLN561 |
A | GLY574 |
A | SER1184 |
A | SER1185 |
A | HOH4213 |
A | HOH4336 |
A | HOH4588 |
site_id | BC8 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL B 4007 |
Chain | Residue |
B | ARG839 |
B | HIS840 |
B | ILE877 |
B | THR909 |
B | ALA910 |
B | PHE911 |
B | GLY913 |
B | PHE914 |
B | GLY915 |
B | GLN918 |
site_id | BC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 4008 |
Chain | Residue |
B | GLN561 |
B | GLY574 |
B | SER1184 |
B | SER1185 |
B | HOH4234 |
B | HOH4355 |
B | HOH4595 |
B | HOH5009 |
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. GFggKetrstlvsvava..LaayKTghpVrCmlDRneD |
Chain | Residue | Details |
A | GLY797-ASP832 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:15148401 |
Chain | Residue | Details |
A | GLU1261 | |
B | GLU1261 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401, ECO:0000269|PubMed:19109252 |
Chain | Residue | Details |
A | CYS43 | |
A | PHE798 | |
A | ARG912 | |
A | ALA1079 | |
B | CYS43 | |
B | CYS48 | |
B | CYS51 | |
B | CYS73 | |
B | CYS113 | |
B | CYS116 | |
B | CYS148 | |
A | CYS48 | |
B | CYS150 | |
B | GLN767 | |
B | PHE798 | |
B | ARG912 | |
B | ALA1079 | |
A | CYS51 | |
A | CYS73 | |
A | CYS113 | |
A | CYS116 | |
A | CYS148 | |
A | CYS150 | |
A | GLN767 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401 |
Chain | Residue | Details |
A | LEU257 | |
B | ASP360 | |
B | LEU404 | |
B | LYS422 | |
A | PHE337 | |
A | SER347 | |
A | ASP360 | |
A | LEU404 | |
A | LYS422 | |
B | LEU257 | |
B | PHE337 | |
B | SER347 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU802 | |
A | ARG880 | |
A | PHE914 | |
A | THR1010 | |
B | GLU802 | |
B | ARG880 | |
B | PHE914 | |
B | THR1010 |
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 | 1 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
B | GLU1261 |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
A | ARG912 | |
A | GLN767 |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1fiq |
Chain | Residue | Details |
B | ARG912 | |
B | GLN767 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 139 |
Chain | Residue | Details |
A | GLU802 | electrostatic stabiliser, hydrogen bond acceptor |
A | ARG880 | electrostatic stabiliser, hydrogen bond donor |
A | GLU1261 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 139 |
Chain | Residue | Details |
B | GLU802 | electrostatic stabiliser, hydrogen bond acceptor |
B | ARG880 | electrostatic stabiliser, hydrogen bond donor |
B | GLU1261 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |