3LKT
Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through Catalysis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0008199 | molecular_function | ferric iron binding |
| A | 0009056 | biological_process | catabolic process |
| A | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| A | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| A | 0042952 | biological_process | beta-ketoadipate pathway |
| A | 0051213 | molecular_function | dioxygenase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005506 | molecular_function | iron ion binding |
| B | 0008199 | molecular_function | ferric iron binding |
| B | 0009056 | biological_process | catabolic process |
| B | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| B | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| B | 0042952 | biological_process | beta-ketoadipate pathway |
| B | 0051213 | molecular_function | dioxygenase activity |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005506 | molecular_function | iron ion binding |
| C | 0008199 | molecular_function | ferric iron binding |
| C | 0009056 | biological_process | catabolic process |
| C | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| C | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| C | 0042952 | biological_process | beta-ketoadipate pathway |
| C | 0051213 | molecular_function | dioxygenase activity |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005506 | molecular_function | iron ion binding |
| D | 0008199 | molecular_function | ferric iron binding |
| D | 0009056 | biological_process | catabolic process |
| D | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| D | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| D | 0042952 | biological_process | beta-ketoadipate pathway |
| D | 0051213 | molecular_function | dioxygenase activity |
| E | 0003824 | molecular_function | catalytic activity |
| E | 0005506 | molecular_function | iron ion binding |
| E | 0008199 | molecular_function | ferric iron binding |
| E | 0009056 | biological_process | catabolic process |
| E | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| E | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| E | 0042952 | biological_process | beta-ketoadipate pathway |
| E | 0051213 | molecular_function | dioxygenase activity |
| F | 0003824 | molecular_function | catalytic activity |
| F | 0005506 | molecular_function | iron ion binding |
| F | 0008199 | molecular_function | ferric iron binding |
| F | 0009056 | biological_process | catabolic process |
| F | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| F | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| F | 0042952 | biological_process | beta-ketoadipate pathway |
| F | 0051213 | molecular_function | dioxygenase activity |
| M | 0003824 | molecular_function | catalytic activity |
| M | 0005506 | molecular_function | iron ion binding |
| M | 0008199 | molecular_function | ferric iron binding |
| M | 0009056 | biological_process | catabolic process |
| M | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| M | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| M | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| M | 0042952 | biological_process | beta-ketoadipate pathway |
| M | 0046872 | molecular_function | metal ion binding |
| M | 0051213 | molecular_function | dioxygenase activity |
| N | 0003824 | molecular_function | catalytic activity |
| N | 0005506 | molecular_function | iron ion binding |
| N | 0008199 | molecular_function | ferric iron binding |
| N | 0009056 | biological_process | catabolic process |
| N | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| N | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| N | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| N | 0042952 | biological_process | beta-ketoadipate pathway |
| N | 0046872 | molecular_function | metal ion binding |
| N | 0051213 | molecular_function | dioxygenase activity |
| O | 0003824 | molecular_function | catalytic activity |
| O | 0005506 | molecular_function | iron ion binding |
| O | 0008199 | molecular_function | ferric iron binding |
| O | 0009056 | biological_process | catabolic process |
| O | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| O | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| O | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| O | 0042952 | biological_process | beta-ketoadipate pathway |
| O | 0046872 | molecular_function | metal ion binding |
| O | 0051213 | molecular_function | dioxygenase activity |
| P | 0003824 | molecular_function | catalytic activity |
| P | 0005506 | molecular_function | iron ion binding |
| P | 0008199 | molecular_function | ferric iron binding |
| P | 0009056 | biological_process | catabolic process |
| P | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| P | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| P | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| P | 0042952 | biological_process | beta-ketoadipate pathway |
| P | 0046872 | molecular_function | metal ion binding |
| P | 0051213 | molecular_function | dioxygenase activity |
| Q | 0003824 | molecular_function | catalytic activity |
| Q | 0005506 | molecular_function | iron ion binding |
| Q | 0008199 | molecular_function | ferric iron binding |
| Q | 0009056 | biological_process | catabolic process |
| Q | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| Q | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| Q | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| Q | 0042952 | biological_process | beta-ketoadipate pathway |
| Q | 0046872 | molecular_function | metal ion binding |
| Q | 0051213 | molecular_function | dioxygenase activity |
| R | 0003824 | molecular_function | catalytic activity |
| R | 0005506 | molecular_function | iron ion binding |
| R | 0008199 | molecular_function | ferric iron binding |
| R | 0009056 | biological_process | catabolic process |
| R | 0016702 | molecular_function | oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen |
| R | 0018578 | molecular_function | protocatechuate 3,4-dioxygenase activity |
| R | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| R | 0042952 | biological_process | beta-ketoadipate pathway |
| R | 0046872 | molecular_function | metal ion binding |
| R | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 201 |
| Chain | Residue |
| A | ASN37 |
| A | THR105 |
| A | HIS107 |
| A | HOH1777 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME A 202 |
| Chain | Residue |
| A | GLY191 |
| A | GLU192 |
| A | HOH2075 |
| A | TYR56 |
| A | ASP57 |
| A | ARG188 |
| A | ILE189 |
| A | GLN190 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS A 203 |
| Chain | Residue |
| A | THR169 |
| A | ILE171 |
| A | ARG184 |
| A | PHE185 |
| A | ASP186 |
| A | ARG188 |
| A | HOH2346 |
| A | HOH2672 |
| A | HOH2673 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE M 600 |
| Chain | Residue |
| M | BME29 |
| M | TYR408 |
| M | HIS460 |
| M | HIS462 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL M 7 |
| Chain | Residue |
| M | LYS325 |
| M | ILE328 |
| M | ALA329 |
| M | HOH2298 |
| M | HOH2546 |
| O | HOH38 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL M 8 |
| Chain | Residue |
| M | HIS534 |
| M | PHE535 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL M 9 |
| Chain | Residue |
| M | CYS429 |
| M | LEU430 |
| M | HOH931 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL M 14 |
| Chain | Residue |
| M | ARG383 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL M 16 |
| Chain | Residue |
| M | GLN503 |
| M | ILE505 |
| M | LYS507 |
| M | ARG522 |
| M | PHE523 |
| M | ASP524 |
| site_id | BC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BME M 21 |
| Chain | Residue |
| A | PRO15 |
| A | ARG133 |
| M | BME29 |
| M | TYR324 |
| M | THR326 |
| M | TRP449 |
| M | ILE491 |
| M | HOH874 |
| M | HOH2281 |
| M | HOH2282 |
| M | HOH2291 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BME M 29 |
| Chain | Residue |
| A | PRO15 |
| A | TYR16 |
| M | BME21 |
| M | HOH225 |
| M | TYR408 |
| M | ARG457 |
| M | HIS460 |
| M | HIS462 |
| M | FE600 |
| site_id | BC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME M 36 |
| Chain | Residue |
| M | ILE339 |
| M | PRO340 |
| M | HOH1268 |
| M | HOH2624 |
| M | HOH2651 |
| N | ARG450 |
| N | PRO453 |
| Q | PRO515 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME M 47 |
| Chain | Residue |
| M | ARG409 |
| M | PRO421 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 201 |
| Chain | Residue |
| B | ASN37 |
| B | THR105 |
| B | HIS107 |
| site_id | BC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE TRS B 202 |
| Chain | Residue |
| B | GLU168 |
| B | THR169 |
| B | ILE171 |
| B | ARG184 |
| B | PHE185 |
| B | ASP186 |
| B | ARG188 |
| B | HOH2480 |
| B | HOH2620 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE N 600 |
| Chain | Residue |
| N | BME32 |
| N | TYR408 |
| N | HIS460 |
| N | HIS462 |
| site_id | BC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL N 13 |
| Chain | Residue |
| N | ARG383 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BME N 18 |
| Chain | Residue |
| B | PRO15 |
| B | ARG133 |
| N | TYR324 |
| N | THR326 |
| N | TRP449 |
| N | ILE491 |
| N | HOH542 |
| N | HOH2277 |
| N | HOH2292 |
| site_id | CC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BME N 32 |
| Chain | Residue |
| B | PRO15 |
| B | TYR16 |
| N | TYR408 |
| N | ARG457 |
| N | HIS460 |
| N | HIS462 |
| N | HOH552 |
| N | FE600 |
| N | HOH2285 |
| site_id | CC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE BME N 37 |
| Chain | Residue |
| N | PHE535 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME N 44 |
| Chain | Residue |
| N | GLN503 |
| N | PHE523 |
| N | ASP524 |
| N | HOH2609 |
| site_id | CC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 201 |
| Chain | Residue |
| C | ASN37 |
| C | ARG38 |
| C | THR105 |
| C | HIS107 |
| site_id | CC5 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL C 202 |
| Chain | Residue |
| C | GLU168 |
| C | ILE171 |
| C | ARG184 |
| C | PHE185 |
| C | ASP186 |
| C | ARG188 |
| C | HOH223 |
| site_id | CC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BME C 203 |
| Chain | Residue |
| C | TYR56 |
| C | ASP57 |
| C | ARG188 |
| C | ILE189 |
| C | GLN190 |
| C | GLY191 |
| C | GLU192 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE O 600 |
| Chain | Residue |
| O | BME30 |
| O | TYR408 |
| O | HIS460 |
| O | HIS462 |
| site_id | CC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL O 12 |
| Chain | Residue |
| O | ARG383 |
| site_id | CC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME O 27 |
| Chain | Residue |
| O | PHE535 |
| O | HOH1701 |
| site_id | DC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME O 30 |
| Chain | Residue |
| C | PRO15 |
| C | TYR16 |
| O | TYR408 |
| O | ARG457 |
| O | HIS460 |
| O | HIS462 |
| O | FE600 |
| O | HOH605 |
| site_id | DC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BME O 33 |
| Chain | Residue |
| C | PRO15 |
| C | ARG133 |
| O | HOH253 |
| O | TYR324 |
| O | THR326 |
| O | TRP449 |
| O | ILE491 |
| O | HOH2279 |
| O | HOH2280 |
| site_id | DC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME O 42 |
| Chain | Residue |
| O | HOH44 |
| O | THR321 |
| O | PRO322 |
| O | ASP323 |
| O | HOH559 |
| O | HOH1820 |
| site_id | DC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME O 45 |
| Chain | Residue |
| O | ARG522 |
| O | PHE523 |
| O | ASP524 |
| O | HOH2610 |
| site_id | DC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME O 49 |
| Chain | Residue |
| D | GLU176 |
| O | PHE356 |
| O | CYS429 |
| O | LEU430 |
| O | HOH1460 |
| O | HOH2487 |
| site_id | DC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 201 |
| Chain | Residue |
| D | ASN37 |
| D | THR105 |
| D | HIS107 |
| D | HOH1092 |
| D | HOH1436 |
| site_id | DC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS D 202 |
| Chain | Residue |
| D | THR169 |
| D | ILE171 |
| D | ARG184 |
| D | PHE185 |
| D | ASP186 |
| D | ARG188 |
| D | HOH2590 |
| site_id | DC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE P 600 |
| Chain | Residue |
| P | BME31 |
| P | TYR408 |
| P | HIS460 |
| P | HIS462 |
| site_id | DC9 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL P 15 |
| Chain | Residue |
| P | ARG383 |
| site_id | EC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE BME P 22 |
| Chain | Residue |
| D | GLY14 |
| D | PRO15 |
| D | ARG133 |
| P | TYR324 |
| P | THR326 |
| P | TRP449 |
| P | ILE491 |
| P | HOH811 |
| P | HOH2286 |
| P | HOH2287 |
| P | HOH2650 |
| site_id | EC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME P 23 |
| Chain | Residue |
| P | GLN503 |
| P | ILE505 |
| P | PHE523 |
| P | ASP524 |
| P | HOH2294 |
| P | HOH2393 |
| site_id | EC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME P 25 |
| Chain | Residue |
| P | PHE356 |
| P | CYS429 |
| P | LEU430 |
| P | HOH1204 |
| site_id | EC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME P 31 |
| Chain | Residue |
| D | PRO15 |
| D | TYR16 |
| P | TYR408 |
| P | ARG457 |
| P | HIS460 |
| P | HIS462 |
| P | HOH540 |
| P | FE600 |
| site_id | EC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME P 35 |
| Chain | Residue |
| P | ARG407 |
| P | PRO418 |
| P | LEU419 |
| site_id | EC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME P 40 |
| Chain | Residue |
| P | HOH21 |
| P | ASN454 |
| P | ASP455 |
| P | MET488 |
| R | HOH678 |
| site_id | EC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME P 41 |
| Chain | Residue |
| P | THR533 |
| P | PHE535 |
| site_id | EC8 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME P 48 |
| Chain | Residue |
| P | ARG409 |
| P | PRO421 |
| site_id | EC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 E 201 |
| Chain | Residue |
| E | ASN37 |
| E | THR105 |
| E | HIS107 |
| site_id | FC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE TRS E 202 |
| Chain | Residue |
| E | GLU168 |
| E | THR169 |
| E | ILE171 |
| E | ALA172 |
| E | ARG184 |
| E | PHE185 |
| E | ASP186 |
| E | ARG188 |
| E | HOH2517 |
| E | HOH2621 |
| site_id | FC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE Q 600 |
| Chain | Residue |
| Q | BME34 |
| Q | TYR408 |
| Q | HIS460 |
| Q | HIS462 |
| site_id | FC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL Q 11 |
| Chain | Residue |
| Q | ARG383 |
| site_id | FC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BME Q 19 |
| Chain | Residue |
| E | PRO15 |
| E | ARG133 |
| Q | TYR324 |
| Q | THR326 |
| Q | TRP449 |
| Q | ILE491 |
| Q | HOH626 |
| Q | HOH2278 |
| Q | HOH2452 |
| site_id | FC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME Q 24 |
| Chain | Residue |
| Q | GLN503 |
| Q | PHE523 |
| Q | ASP524 |
| Q | HOH2332 |
| site_id | FC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BME Q 34 |
| Chain | Residue |
| E | PRO15 |
| E | TYR16 |
| Q | HOH251 |
| Q | TYR408 |
| Q | ARG457 |
| Q | HIS460 |
| Q | HIS462 |
| Q | FE600 |
| Q | HOH623 |
| site_id | FC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME Q 46 |
| Chain | Residue |
| Q | PHE356 |
| Q | CYS429 |
| Q | LEU430 |
| Q | HOH1300 |
| site_id | FC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 F 201 |
| Chain | Residue |
| F | ASN37 |
| F | ARG38 |
| F | THR105 |
| F | HIS107 |
| site_id | FC9 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE TRS F 202 |
| Chain | Residue |
| F | THR169 |
| F | ILE171 |
| F | ARG184 |
| F | PHE185 |
| F | ASP186 |
| F | ARG188 |
| F | HOH2665 |
| site_id | GC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE R 600 |
| Chain | Residue |
| R | BME28 |
| R | TYR408 |
| R | HIS460 |
| R | HIS462 |
| site_id | GC2 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL R 10 |
| Chain | Residue |
| R | ARG383 |
| site_id | GC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME R 20 |
| Chain | Residue |
| F | PRO15 |
| F | ARG133 |
| R | HOH188 |
| R | TYR324 |
| R | THR326 |
| R | TRP449 |
| R | HOH2289 |
| R | HOH2290 |
| site_id | GC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME R 26 |
| Chain | Residue |
| R | HIS534 |
| R | PHE535 |
| R | HOH1839 |
| site_id | GC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME R 28 |
| Chain | Residue |
| F | PRO15 |
| F | TYR16 |
| R | HOH35 |
| R | TYR408 |
| R | ARG457 |
| R | HIS460 |
| R | HIS462 |
| R | FE600 |
| site_id | GC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME R 43 |
| Chain | Residue |
| B | ILE2 |
| R | ARG522 |
| R | PHE523 |
| R | ASP524 |
| R | HOH2611 |
Functional Information from PROSITE/UniProt
| site_id | PS00083 |
| Number of Residues | 29 |
| Details | INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. LlGqVydgnGhlVrdsfLEVwqadanGeY |
| Chain | Residue | Details |
| A | LEU51-TYR79 | |
| M | VAL380-TYR408 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7990141 |
| Chain | Residue | Details |
| M | TYR408 | |
| O | HIS447 | |
| O | HIS460 | |
| O | HIS462 | |
| P | TYR408 | |
| P | HIS447 | |
| P | HIS460 | |
| P | HIS462 | |
| Q | TYR408 | |
| Q | HIS447 | |
| Q | HIS460 | |
| M | HIS447 | |
| Q | HIS462 | |
| R | TYR408 | |
| R | HIS447 | |
| R | HIS460 | |
| R | HIS462 | |
| M | HIS460 | |
| M | HIS462 | |
| N | TYR408 | |
| N | HIS447 | |
| N | HIS460 | |
| N | HIS462 | |
| O | TYR408 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| M | TYR408 | metal ligand |
| M | HIS447 | metal ligand, proton shuttle (general acid/base) |
| M | ARG457 | electrostatic stabiliser |
| M | HIS460 | metal ligand |
| M | HIS462 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| N | TYR408 | metal ligand |
| N | HIS447 | metal ligand, proton shuttle (general acid/base) |
| N | ARG457 | electrostatic stabiliser |
| N | HIS460 | metal ligand |
| N | HIS462 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| O | TYR408 | metal ligand |
| O | HIS447 | metal ligand, proton shuttle (general acid/base) |
| O | ARG457 | electrostatic stabiliser |
| O | HIS460 | metal ligand |
| O | HIS462 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| P | TYR408 | metal ligand |
| P | HIS447 | metal ligand, proton shuttle (general acid/base) |
| P | ARG457 | electrostatic stabiliser |
| P | HIS460 | metal ligand |
| P | HIS462 | metal ligand |
| site_id | MCSA5 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| Q | TYR408 | metal ligand |
| Q | HIS447 | metal ligand, proton shuttle (general acid/base) |
| Q | ARG457 | electrostatic stabiliser |
| Q | HIS460 | metal ligand |
| Q | HIS462 | metal ligand |
| site_id | MCSA6 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| R | TYR408 | metal ligand |
| R | HIS447 | metal ligand, proton shuttle (general acid/base) |
| R | ARG457 | electrostatic stabiliser |
| R | HIS460 | metal ligand |
| R | HIS462 | metal ligand |
