1VDV
Bovine Milk Xanthine Dehydrogenase Y-700 Bound Form
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 5301 |
Chain | Residue |
A | ALA867 |
A | SER870 |
A | ARG871 |
A | SER874 |
A | SER907 |
A | ASN908 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 5302 |
Chain | Residue |
B | SER874 |
B | SER907 |
B | ASN908 |
B | ALA867 |
B | SER870 |
B | ARG871 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA B 5303 |
Chain | Residue |
B | HIS741 |
B | TYR743 |
B | THR836 |
B | GLY837 |
B | HOH5367 |
B | HOH6328 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CA A 5304 |
Chain | Residue |
A | HIS741 |
A | TYR743 |
A | THR836 |
A | GLY837 |
A | HOH5508 |
A | HOH6075 |
site_id | AC5 |
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 | AC6 |
Number of Residues | 9 |
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 | CYS73 |
site_id | AC7 |
Number of Residues | 19 |
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 | MOS3004 |
A | HOH5406 |
A | HOH5427 |
A | HOH5585 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MOS A 3004 |
Chain | Residue |
A | GLN767 |
A | GLY799 |
A | PHE911 |
A | ARG912 |
A | ALA1078 |
A | ALA1079 |
A | GLU1261 |
A | MTE3003 |
A | HOH5555 |
site_id | AC9 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD A 3005 |
Chain | Residue |
A | HOH5577 |
A | HOH5915 |
A | HOH6017 |
A | HOH6368 |
A | GLU45 |
A | GLY46 |
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 | ASP430 |
A | GOL5004 |
A | HOH5371 |
site_id | BC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE FES B 4001 |
Chain | Residue |
B | GLN112 |
B | CYS113 |
B | GLY114 |
B | CYS116 |
B | CYS148 |
B | ARG149 |
B | CYS150 |
B | LEU744 |
site_id | BC2 |
Number of Residues | 9 |
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 | CYS73 |
site_id | BC3 |
Number of Residues | 19 |
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 | MOS4004 |
B | HOH5397 |
B | HOH5456 |
B | HOH5481 |
site_id | BC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE MOS B 4004 |
Chain | Residue |
B | GLN767 |
B | GLY799 |
B | PHE911 |
B | ARG912 |
B | ALA1078 |
B | ALA1079 |
B | GLU1261 |
B | MTE4003 |
B | HOH6314 |
site_id | BC5 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD B 4005 |
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 | THR354 |
B | SER359 |
B | ASP360 |
B | ILE403 |
B | LEU404 |
B | LYS422 |
B | ASP429 |
B | ASP430 |
B | GOL5021 |
B | HOH5361 |
B | HOH5706 |
B | HOH5707 |
B | HOH5771 |
site_id | BC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE YSH A 5101 |
Chain | Residue |
A | ASN768 |
A | GLU802 |
A | LEU873 |
A | SER876 |
A | ARG880 |
A | PHE914 |
A | SER1008 |
A | PHE1009 |
A | THR1010 |
A | VAL1011 |
A | PHE1013 |
A | LEU1014 |
A | PRO1076 |
A | ALA1079 |
A | HOH5335 |
A | HOH5555 |
site_id | BC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE YSH B 5102 |
Chain | Residue |
B | ASN768 |
B | GLU802 |
B | LEU873 |
B | SER876 |
B | ARG880 |
B | PHE914 |
B | SER1008 |
B | PHE1009 |
B | THR1010 |
B | VAL1011 |
B | PHE1013 |
B | LEU1014 |
B | PRO1076 |
B | ALA1079 |
B | HOH5556 |
B | HOH6314 |
site_id | BC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 5001 |
Chain | Residue |
A | PHE549 |
A | LYS994 |
A | GLU1163 |
A | ASP1170 |
A | HIS1171 |
A | LYS1172 |
site_id | BC9 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 5002 |
Chain | Residue |
A | THR207 |
A | LEU521 |
A | LEU524 |
A | LYS537 |
A | LEU538 |
A | ASP539 |
A | HOH5542 |
A | HOH5793 |
A | HOH6040 |
site_id | CC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 5003 |
Chain | Residue |
A | TRP336 |
A | LYS422 |
A | GLN423 |
A | ARG427 |
A | ASP1170 |
A | HOH5603 |
A | HOH5853 |
site_id | CC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 5004 |
Chain | Residue |
A | GLU45 |
A | ILE266 |
A | SER1225 |
A | FAD3005 |
A | GOL5005 |
A | HOH5710 |
A | HOH6094 |
site_id | CC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 5005 |
Chain | Residue |
A | GLU45 |
A | ASN830 |
A | ARG1222 |
A | SER1225 |
A | GOL5004 |
A | HOH5506 |
A | HOH6385 |
site_id | CC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 5006 |
Chain | Residue |
A | ASP594 |
A | PHE604 |
A | MET826 |
A | HOH5429 |
A | HOH5462 |
site_id | CC5 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 5007 |
Chain | Residue |
B | THR207 |
B | GLN208 |
B | LEU524 |
B | LYS537 |
B | ASP539 |
B | TYR542 |
site_id | CC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 5008 |
Chain | Residue |
B | PHE549 |
B | LYS994 |
B | GLU1163 |
B | ASP1170 |
B | HIS1171 |
B | LYS1172 |
B | HOH6285 |
site_id | CC7 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 5009 |
Chain | Residue |
B | TRP336 |
B | LYS422 |
B | GLN423 |
B | ARG427 |
B | ASP1170 |
B | GOL5022 |
B | HOH5487 |
B | HOH5570 |
B | HOH5644 |
site_id | CC8 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL A 5011 |
Chain | Residue |
A | GLU759 |
A | ASN785 |
A | ARG786 |
A | ILE787 |
A | LEU788 |
A | HOH5551 |
B | LEU1030 |
B | SER1064 |
site_id | CC9 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 5012 |
Chain | Residue |
B | LEU580 |
B | ALA581 |
B | VAL1047 |
B | TYR1062 |
B | ILE1063 |
B | HOH5461 |
B | HOH5598 |
B | HOH5735 |
site_id | DC1 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 5013 |
Chain | Residue |
B | ARG31 |
B | ARG37 |
B | ASP594 |
B | ASP595 |
B | ILE596 |
B | ARG824 |
B | GOL5014 |
B | HOH5396 |
site_id | DC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE GOL B 5014 |
Chain | Residue |
B | ASP594 |
B | PHE604 |
B | PRO675 |
B | MET826 |
B | GOL5013 |
B | HOH5576 |
B | HOH6239 |
B | HOH6331 |
site_id | DC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 5015 |
Chain | Residue |
B | HIS665 |
B | ILE666 |
B | ARG804 |
B | ILE835 |
B | ASN869 |
B | SER906 |
B | SER907 |
B | HOH5767 |
B | HOH6010 |
site_id | DC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL A 5016 |
Chain | Residue |
A | LEU580 |
A | ALA581 |
A | VAL1047 |
A | TYR1062 |
A | ILE1063 |
A | HOH5764 |
site_id | DC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL A 5017 |
Chain | Residue |
A | GLN561 |
A | GLY574 |
A | SER1184 |
A | SER1185 |
A | HOH5490 |
site_id | DC6 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 5018 |
Chain | Residue |
A | GLY664 |
A | HIS665 |
A | ILE666 |
A | ARG804 |
A | ILE835 |
A | ASN869 |
A | SER906 |
A | SER907 |
A | HOH5774 |
A | HOH5951 |
site_id | DC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 5019 |
Chain | Residue |
A | ARG606 |
A | LEU607 |
A | VAL608 |
A | THR609 |
A | HIS683 |
A | HOH5564 |
A | HOH5998 |
site_id | DC8 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE GOL B 5020 |
Chain | Residue |
B | GLU45 |
B | ILE266 |
B | LYS271 |
B | GOL5021 |
site_id | DC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE GOL B 5021 |
Chain | Residue |
B | ILE266 |
B | SER1225 |
B | FAD4005 |
B | GOL5020 |
B | HOH5634 |
site_id | EC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 5022 |
Chain | Residue |
B | GLU332 |
B | PHE421 |
B | LYS518 |
B | LEU548 |
B | PHE549 |
B | GOL5009 |
B | HOH5457 |
site_id | EC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACY A 5201 |
Chain | Residue |
A | ARG839 |
A | HIS840 |
A | ILE877 |
A | THR909 |
A | ALA910 |
A | PHE911 |
A | PHE914 |
A | GLY915 |
A | GLN918 |
site_id | EC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE ACY B 5202 |
Chain | Residue |
B | ARG839 |
B | HIS840 |
B | ILE877 |
B | THR909 |
B | ALA910 |
B | PHE911 |
B | PHE914 |
B | GLY915 |
B | GLN918 |
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 | PRO1262 | |
B | PRO1262 |
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 | GLY44 | |
A | GLY799 | |
A | GLY913 | |
A | SER1080 | |
B | GLY44 | |
B | GLY49 | |
B | THR52 | |
B | LEU74 | |
B | GLY114 | |
B | THR117 | |
B | ARG149 | |
A | GLY49 | |
B | THR151 | |
B | ASN768 | |
B | GLY799 | |
B | GLY913 | |
B | SER1080 | |
A | THR52 | |
A | LEU74 | |
A | GLY114 | |
A | THR117 | |
A | ARG149 | |
A | THR151 | |
A | ASN768 |
site_id | SWS_FT_FI3 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12421831, ECO:0000269|PubMed:15148401 |
Chain | Residue | Details |
A | VAL258 | |
B | LEU361 | |
B | LEU405 | |
B | GLN423 | |
A | ALA338 | |
A | LEU348 | |
A | LEU361 | |
A | LEU405 | |
A | GLN423 | |
B | VAL258 | |
B | ALA338 | |
B | LEU348 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
A | THR803 | |
A | ALA881 | |
A | GLY915 | |
A | VAL1011 | |
B | THR803 | |
B | ALA881 | |
B | GLY915 | |
B | VAL1011 |
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 | THR803 | electrostatic stabiliser, hydrogen bond acceptor |
A | ALA881 | electrostatic stabiliser, hydrogen bond donor |
A | PRO1262 | 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 | THR803 | electrostatic stabiliser, hydrogen bond acceptor |
B | ALA881 | electrostatic stabiliser, hydrogen bond donor |
B | PRO1262 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |