1JRO
Crystal Structure of Xanthine Dehydrogenase from Rhodobacter capsulatus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004854 | molecular_function | xanthine dehydrogenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0005506 | molecular_function | iron ion binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0030151 | molecular_function | molybdenum ion binding |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0004854 | molecular_function | xanthine dehydrogenase activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| C | 0071949 | molecular_function | FAD binding |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0030151 | molecular_function | molybdenum ion binding |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0004854 | molecular_function | xanthine dehydrogenase activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0046872 | molecular_function | metal ion binding |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0051536 | molecular_function | iron-sulfur cluster binding |
| E | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| E | 0071949 | molecular_function | FAD binding |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0030151 | molecular_function | molybdenum ion binding |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000166 | molecular_function | nucleotide binding |
| G | 0004854 | molecular_function | xanthine dehydrogenase activity |
| G | 0005506 | molecular_function | iron ion binding |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0046872 | molecular_function | metal ion binding |
| G | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| G | 0051536 | molecular_function | iron-sulfur cluster binding |
| G | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| G | 0071949 | molecular_function | FAD binding |
| H | 0005506 | molecular_function | iron ion binding |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0030151 | molecular_function | molybdenum ion binding |
| H | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA B 3006 |
| Chain | Residue |
| B | GLU172 |
| B | HIS173 |
| B | TYR175 |
| B | THR266 |
| B | GLY267 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA D 3006 |
| Chain | Residue |
| D | GLY267 |
| D | GLU172 |
| D | HIS173 |
| D | TYR175 |
| D | THR266 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA F 3006 |
| Chain | Residue |
| F | GLU172 |
| F | HIS173 |
| F | TYR175 |
| F | THR266 |
| F | GLY267 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA H 3006 |
| Chain | Residue |
| H | GLU172 |
| H | HIS173 |
| H | TYR175 |
| H | THR266 |
| H | GLY267 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 3001 |
| Chain | Residue |
| A | GLN102 |
| A | CYS103 |
| A | GLY104 |
| A | CYS106 |
| A | CYS134 |
| A | ARG135 |
| A | CYS136 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES A 3002 |
| Chain | Residue |
| A | GLY38 |
| A | CYS39 |
| A | ASN40 |
| A | GLY42 |
| A | CYS44 |
| A | GLY45 |
| A | CYS47 |
| A | ASN61 |
| A | CYS63 |
| site_id | AC7 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MTE B 3003 |
| Chain | Residue |
| A | GLN102 |
| A | CYS136 |
| B | GLY226 |
| B | GLY227 |
| B | PHE228 |
| B | ARG342 |
| B | MET488 |
| B | GLY489 |
| B | GLN490 |
| B | THR527 |
| B | ALA528 |
| B | ALA529 |
| B | SER530 |
| B | SER531 |
| B | GLY532 |
| B | ALA533 |
| B | GLN663 |
| B | GLU730 |
| B | MOS3004 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MOS B 3004 |
| Chain | Residue |
| B | GLN197 |
| B | GLY229 |
| B | PHE341 |
| B | ARG342 |
| B | ALA528 |
| B | ALA529 |
| B | GLU730 |
| B | MTE3003 |
| site_id | AC9 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD A 3005 |
| Chain | Residue |
| A | GLU41 |
| A | GLY42 |
| A | ASP43 |
| A | LEU201 |
| A | ALA203 |
| A | GLY204 |
| A | GLY205 |
| A | THR206 |
| A | ASP207 |
| A | VAL208 |
| A | TRP211 |
| A | PHE270 |
| A | ALA271 |
| A | ALA279 |
| A | THR280 |
| A | GLY283 |
| A | ASN284 |
| A | ALA286 |
| A | GLY292 |
| A | ASP293 |
| A | ARG330 |
| A | PHE335 |
| A | VAL336 |
| A | LYS352 |
| A | GLN359 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES C 3001 |
| Chain | Residue |
| C | GLN102 |
| C | CYS103 |
| C | GLY104 |
| C | CYS106 |
| C | CYS134 |
| C | ARG135 |
| C | CYS136 |
| site_id | BC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES C 3002 |
| Chain | Residue |
| C | CYS44 |
| C | GLY45 |
| C | CYS47 |
| C | CYS63 |
| C | GLY38 |
| C | CYS39 |
| C | ASN40 |
| C | GLY42 |
| site_id | BC3 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MTE D 3003 |
| Chain | Residue |
| C | GLN102 |
| C | CYS136 |
| D | GLY226 |
| D | GLY227 |
| D | PHE228 |
| D | ARG342 |
| D | MET488 |
| D | GLY489 |
| D | GLN490 |
| D | THR527 |
| D | ALA528 |
| D | ALA529 |
| D | SER530 |
| D | SER531 |
| D | GLY532 |
| D | ALA533 |
| D | GLN663 |
| D | GLU730 |
| D | MOS3004 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE MOS D 3004 |
| Chain | Residue |
| D | GLN197 |
| D | GLY229 |
| D | PHE341 |
| D | ARG342 |
| D | ALA528 |
| D | ALA529 |
| D | GLU730 |
| D | MTE3003 |
| site_id | BC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD C 3005 |
| Chain | Residue |
| C | GLU41 |
| C | GLY42 |
| C | ASP43 |
| C | LEU201 |
| C | ALA203 |
| C | GLY204 |
| C | GLY205 |
| C | THR206 |
| C | ASP207 |
| C | VAL208 |
| C | PHE270 |
| C | ALA271 |
| C | ALA279 |
| C | THR280 |
| C | ASN284 |
| C | ALA286 |
| C | GLY292 |
| C | ASP293 |
| C | ARG330 |
| C | PHE335 |
| C | VAL336 |
| C | LYS352 |
| C | GLN359 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES E 3001 |
| Chain | Residue |
| E | GLN102 |
| E | CYS103 |
| E | GLY104 |
| E | CYS106 |
| E | CYS134 |
| E | ARG135 |
| E | CYS136 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE FES E 3002 |
| Chain | Residue |
| E | GLY38 |
| E | CYS39 |
| E | ASN40 |
| E | GLY42 |
| E | ASP43 |
| E | CYS44 |
| E | GLY45 |
| E | CYS47 |
| E | CYS63 |
| site_id | BC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE MTE F 3003 |
| Chain | Residue |
| E | GLN102 |
| E | CYS136 |
| F | GLY226 |
| F | GLY227 |
| F | PHE228 |
| F | GLY229 |
| F | ARG342 |
| F | MET488 |
| F | GLY489 |
| F | GLN490 |
| F | THR527 |
| F | ALA529 |
| F | SER530 |
| F | SER531 |
| F | GLY532 |
| F | ALA533 |
| F | GLN663 |
| F | GLU730 |
| F | MOS3004 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MOS F 3004 |
| Chain | Residue |
| F | GLN197 |
| F | GLY229 |
| F | PHE341 |
| F | ARG342 |
| F | GLY343 |
| F | ALA528 |
| F | ALA529 |
| F | GLU730 |
| F | MTE3003 |
| site_id | CC1 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE FAD E 3005 |
| Chain | Residue |
| E | LEU201 |
| E | ALA203 |
| E | GLY204 |
| E | GLY205 |
| E | THR206 |
| E | ASP207 |
| E | VAL208 |
| E | LEU225 |
| E | PHE270 |
| E | ALA271 |
| E | ALA279 |
| E | THR280 |
| E | GLY283 |
| E | ASN284 |
| E | ALA286 |
| E | ASN287 |
| E | GLY292 |
| E | ASP293 |
| E | ARG330 |
| E | PHE335 |
| E | VAL336 |
| E | LYS352 |
| E | GLN359 |
| E | ASP360 |
| site_id | CC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES G 3001 |
| Chain | Residue |
| G | GLN102 |
| G | CYS103 |
| G | CYS106 |
| G | CYS134 |
| G | ARG135 |
| G | CYS136 |
| site_id | CC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES G 3002 |
| Chain | Residue |
| G | GLY38 |
| G | CYS39 |
| G | ASN40 |
| G | GLY42 |
| G | CYS44 |
| G | GLY45 |
| G | CYS47 |
| G | CYS63 |
| site_id | CC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE MTE H 3003 |
| Chain | Residue |
| G | GLN102 |
| G | CYS136 |
| H | GLY226 |
| H | GLY227 |
| H | PHE228 |
| H | GLY229 |
| H | ARG342 |
| H | MET488 |
| H | GLY489 |
| H | GLN490 |
| H | THR527 |
| H | ALA528 |
| H | ALA529 |
| H | SER530 |
| H | SER531 |
| H | GLY532 |
| H | ALA533 |
| H | GLN663 |
| H | GLU730 |
| H | MOS3004 |
| site_id | CC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE MOS H 3004 |
| Chain | Residue |
| H | GLN197 |
| H | PHE228 |
| H | GLY229 |
| H | PHE341 |
| H | ARG342 |
| H | ALA528 |
| H | ALA529 |
| H | GLU730 |
| H | MTE3003 |
| site_id | CC6 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD G 3005 |
| Chain | Residue |
| G | GLY42 |
| G | LEU201 |
| G | ALA203 |
| G | GLY204 |
| G | GLY205 |
| G | THR206 |
| G | ASP207 |
| G | VAL208 |
| G | PHE270 |
| G | ALA271 |
| G | VAL275 |
| G | ALA279 |
| G | THR280 |
| G | ASN284 |
| G | ALA286 |
| G | GLY292 |
| G | ASP293 |
| G | ARG330 |
| G | PHE335 |
| G | VAL336 |
| G | LYS352 |
| G | GLN359 |
| G | ASP360 |
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. CNEGDCGAC |
| Chain | Residue | Details |
| A | CYS39-CYS47 |
Catalytic Information from CSA
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| H | ARG342 | |
| H | GLN197 |
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| B | GLU730 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| D | GLU730 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| F | GLU730 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| H | GLU730 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| B | ARG342 | |
| B | GLN197 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| D | ARG342 | |
| D | GLN197 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1fiq |
| Chain | Residue | Details |
| F | ARG342 | |
| F | GLN197 |
