3PCN
STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 3,4-DIHYDROXYPHENYLACETATE
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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0016491 | molecular_function | oxidoreductase activity |
| 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 FE M 600 |
| Chain | Residue |
| M | TYR408 |
| M | HIS460 |
| M | HIS462 |
| M | DHY550 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE N 600 |
| Chain | Residue |
| N | TYR408 |
| N | HIS460 |
| N | HIS462 |
| N | DHY550 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE O 600 |
| Chain | Residue |
| O | TYR408 |
| O | HIS460 |
| O | HIS462 |
| O | DHY550 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE P 600 |
| Chain | Residue |
| P | TYR408 |
| P | HIS460 |
| P | HIS462 |
| P | DHY550 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE Q 600 |
| Chain | Residue |
| Q | TYR408 |
| Q | HIS460 |
| Q | HIS462 |
| Q | DHY550 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE R 600 |
| Chain | Residue |
| R | TYR408 |
| R | HIS460 |
| R | HIS462 |
| R | DHY550 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME M 601 |
| Chain | Residue |
| M | HIS361 |
| M | CYS429 |
| M | SER438 |
| M | HOH689 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE DHY M 550 |
| Chain | Residue |
| A | PRO15 |
| A | TYR16 |
| M | TYR324 |
| M | TYR408 |
| M | TYR447 |
| M | TRP449 |
| M | ARG457 |
| M | HIS460 |
| M | HIS462 |
| M | GLN477 |
| M | ILE491 |
| M | FE600 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME N 601 |
| Chain | Residue |
| N | HIS361 |
| N | CYS429 |
| N | SER438 |
| N | HOH697 |
| site_id | ACA |
| Number of Residues | 29 |
| Details | SITE "ACA" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS A AND M. |
| Chain | Residue |
| A | THR12 |
| M | TRP400 |
| M | TYR408 |
| M | ASP413 |
| M | TYR447 |
| M | PRO448 |
| M | TRP449 |
| M | ARG450 |
| M | ARG457 |
| M | HIS460 |
| M | HIS462 |
| A | ALA13 |
| M | GLN477 |
| M | ILE491 |
| M | DHY550 |
| M | FE600 |
| M | HOH603 |
| A | HOH204 |
| M | HOH623 |
| M | HOH630 |
| M | HOH631 |
| M | HOH737 |
| A | GLY14 |
| A | PRO15 |
| A | TYR16 |
| A | ARG133 |
| A | GLY134 |
| M | TYR324 |
| M | THR326 |
| site_id | ACB |
| Number of Residues | 29 |
| Details | SITE "ACB" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. |
| Chain | Residue |
| B | THR12 |
| B | ALA13 |
| B | GLY14 |
| B | PRO15 |
| B | TYR16 |
| B | ARG133 |
| B | GLY134 |
| N | TYR324 |
| N | THR326 |
| N | TRP400 |
| N | TYR408 |
| N | ASP413 |
| N | TYR447 |
| N | PRO448 |
| N | TRP449 |
| N | ARG450 |
| N | ARG457 |
| N | HIS460 |
| N | HIS462 |
| N | GLN477 |
| N | ILE491 |
| N | DHY550 |
| N | FE600 |
| N | HOH606 |
| B | HOH235 |
| N | HOH629 |
| N | HOH637 |
| N | HOH638 |
| N | HOH749 |
| site_id | ACC |
| Number of Residues | 29 |
| Details | SITE "ACC" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS C AND O. |
| Chain | Residue |
| C | THR12 |
| C | ALA13 |
| C | GLY14 |
| C | PRO15 |
| C | TYR16 |
| C | ARG133 |
| C | GLY134 |
| O | TYR324 |
| O | THR326 |
| O | TRP400 |
| O | TYR408 |
| O | ASP413 |
| O | TYR447 |
| O | PRO448 |
| O | TRP449 |
| O | ARG450 |
| O | ARG457 |
| O | HIS460 |
| O | HIS462 |
| O | GLN477 |
| O | ILE491 |
| O | DHY550 |
| O | FE600 |
| C | HOH206 |
| C | HOH207 |
| O | HOH628 |
| O | HOH637 |
| O | HOH638 |
| O | HOH748 |
| site_id | ACD |
| Number of Residues | 29 |
| Details | SITE "ACD" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS D AND P. |
| Chain | Residue |
| P | TYR447 |
| P | PRO448 |
| P | TRP449 |
| P | ARG450 |
| P | ARG457 |
| P | HIS460 |
| P | HIS462 |
| P | GLN477 |
| P | ILE491 |
| P | DHY550 |
| P | FE600 |
| D | HOH692 |
| D | HOH693 |
| P | HOH627 |
| P | HOH635 |
| P | HOH636 |
| P | HOH740 |
| D | THR12 |
| D | ALA13 |
| D | GLY14 |
| D | PRO15 |
| D | TYR16 |
| D | ARG133 |
| D | GLY134 |
| P | TYR324 |
| P | THR326 |
| P | TRP400 |
| P | TYR408 |
| P | ASP413 |
| site_id | ACE |
| Number of Residues | 29 |
| Details | SITE "ACE" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS E AND Q. |
| Chain | Residue |
| E | THR12 |
| E | ALA13 |
| E | GLY14 |
| E | PRO15 |
| E | TYR16 |
| E | ARG133 |
| E | GLY134 |
| Q | TYR324 |
| Q | THR326 |
| Q | TRP400 |
| Q | TYR408 |
| Q | ASP413 |
| Q | TYR447 |
| Q | PRO448 |
| Q | TRP449 |
| Q | ARG450 |
| Q | ARG457 |
| Q | HIS460 |
| Q | HIS462 |
| Q | GLN477 |
| Q | ILE491 |
| Q | DHY550 |
| Q | FE600 |
| E | HOH204 |
| E | HOH205 |
| Q | HOH959 |
| Q | HOH974 |
| Q | HOH975 |
| Q | HOH1145 |
| site_id | ACF |
| Number of Residues | 29 |
| Details | SITE "ACF" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS F AND R. |
| Chain | Residue |
| F | THR12 |
| F | ALA13 |
| F | GLY14 |
| F | PRO15 |
| F | TYR16 |
| F | ARG133 |
| F | GLY134 |
| R | TYR324 |
| R | THR326 |
| R | TRP400 |
| R | TYR408 |
| R | ASP413 |
| R | TYR447 |
| R | PRO448 |
| R | TRP449 |
| R | ARG450 |
| R | ARG457 |
| R | HIS460 |
| R | HIS462 |
| R | GLN477 |
| R | ILE491 |
| R | DHY550 |
| R | FE600 |
| F | HOH1150 |
| F | HOH1151 |
| R | HOH1188 |
| R | HOH1203 |
| R | HOH1204 |
| R | HOH1374 |
| site_id | BC1 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE DHY N 550 |
| Chain | Residue |
| B | PRO15 |
| B | TYR16 |
| B | ARG133 |
| N | TYR324 |
| N | TYR408 |
| N | TYR447 |
| N | TRP449 |
| N | ARG457 |
| N | HIS460 |
| N | HIS462 |
| N | ILE491 |
| N | FE600 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME O 601 |
| Chain | Residue |
| O | HIS361 |
| O | CYS429 |
| O | SER438 |
| O | HOH695 |
| site_id | BC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DHY O 550 |
| Chain | Residue |
| C | PRO15 |
| C | TYR16 |
| O | TYR324 |
| O | TYR408 |
| O | TYR447 |
| O | TRP449 |
| O | ARG457 |
| O | HIS460 |
| O | HIS462 |
| O | ILE491 |
| O | FE600 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME P 601 |
| Chain | Residue |
| P | HIS361 |
| P | CYS429 |
| P | SER438 |
| P | HOH691 |
| site_id | BC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DHY P 550 |
| Chain | Residue |
| D | PRO15 |
| D | TYR16 |
| P | TYR324 |
| P | TYR408 |
| P | TRP449 |
| P | ARG457 |
| P | HIS460 |
| P | HIS462 |
| P | ILE491 |
| P | FE600 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME Q 601 |
| Chain | Residue |
| Q | HIS361 |
| Q | CYS429 |
| Q | SER438 |
| Q | HOH1062 |
| site_id | BC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE DHY Q 550 |
| Chain | Residue |
| Q | TYR324 |
| Q | TYR408 |
| Q | TYR447 |
| Q | TRP449 |
| Q | ARG457 |
| Q | HIS460 |
| Q | HIS462 |
| Q | GLN477 |
| Q | ILE491 |
| Q | FE600 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME R 601 |
| Chain | Residue |
| R | HIS361 |
| R | CYS429 |
| R | SER438 |
| R | HOH1291 |
| site_id | BC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE DHY R 550 |
| Chain | Residue |
| F | TYR16 |
| R | TYR324 |
| R | TYR408 |
| R | TYR447 |
| R | TRP449 |
| R | ARG457 |
| R | HIS460 |
| R | HIS462 |
| R | GLN477 |
| R | ILE491 |
| R | FE600 |
| site_id | VEA |
| Number of Residues | 29 |
| Details | SITE "VEA" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS A AND M. |
| Chain | Residue |
| A | TYR79 |
| A | VAL114 |
| A | ASN115 |
| A | ASN116 |
| A | ALA117 |
| A | ALA118 |
| A | MET122 |
| A | HIS125 |
| A | ASN127 |
| A | ARG142 |
| A | VAL157 |
| M | ASP304 |
| M | ARG307 |
| M | ILE339 |
| M | PRO340 |
| M | GLN341 |
| M | SER342 |
| M | ILE343 |
| M | SER344 |
| M | GLU345 |
| A | HOH220 |
| A | HOH223 |
| M | HOH635 |
| A | HOH231 |
| M | HOH642 |
| A | HOH234 |
| M | HOH658 |
| A | HOH245 |
| A | HOH266 |
| site_id | VEB |
| Number of Residues | 29 |
| Details | SITE "VEB" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS B AND N. |
| Chain | Residue |
| B | TYR79 |
| B | VAL114 |
| B | ASN115 |
| B | ASN116 |
| B | ALA117 |
| B | ALA118 |
| B | MET122 |
| B | HIS125 |
| B | ASN127 |
| B | ARG142 |
| B | VAL157 |
| N | ASP304 |
| N | ARG307 |
| N | ILE339 |
| N | PRO340 |
| N | GLN341 |
| N | SER342 |
| N | ILE343 |
| N | SER344 |
| N | GLU345 |
| B | HOH275 |
| B | HOH283 |
| B | HOH294 |
| B | HOH301 |
| N | HOH649 |
| N | HOH651 |
| N | HOH664 |
| N | HOH680 |
| B | HOH419 |
| site_id | VEC |
| Number of Residues | 29 |
| Details | SITE "VEC" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS C AND O. |
| Chain | Residue |
| C | TYR79 |
| C | VAL114 |
| C | ASN115 |
| C | ASN116 |
| C | ALA117 |
| C | ALA118 |
| C | MET122 |
| C | HIS125 |
| C | ASN127 |
| C | ARG142 |
| C | VAL157 |
| O | ASP304 |
| O | ARG307 |
| O | ILE339 |
| O | PRO340 |
| O | GLN341 |
| O | SER342 |
| O | ILE343 |
| O | SER344 |
| O | GLU345 |
| C | HOH223 |
| O | HOH635 |
| C | HOH230 |
| C | HOH234 |
| O | HOH649 |
| C | HOH237 |
| O | HOH663 |
| C | HOH249 |
| O | HOH722 |
| site_id | VED |
| Number of Residues | 29 |
| Details | SITE "VED" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS D AND P. |
| Chain | Residue |
| D | TYR79 |
| D | VAL114 |
| D | ASN115 |
| D | ASN116 |
| D | ALA117 |
| D | ALA118 |
| D | MET122 |
| D | HIS125 |
| D | ASN127 |
| D | ARG142 |
| D | VAL157 |
| P | ASP304 |
| P | ARG307 |
| P | ILE339 |
| P | PRO340 |
| P | GLN341 |
| P | SER342 |
| P | ILE343 |
| P | SER344 |
| P | GLU345 |
| D | HOH733 |
| P | HOH633 |
| D | HOH752 |
| D | HOH759 |
| P | HOH646 |
| D | HOH768 |
| P | HOH662 |
| D | HOH809 |
| D | HOH877 |
| site_id | VEE |
| Number of Residues | 29 |
| Details | SITE "VEE" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS E AND Q. |
| Chain | Residue |
| E | TYR79 |
| E | VAL114 |
| E | ASN115 |
| E | ASN116 |
| E | ALA117 |
| E | ALA118 |
| E | MET122 |
| E | HIS125 |
| E | ASN127 |
| E | ARG142 |
| E | VAL157 |
| Q | ASP304 |
| Q | ARG307 |
| Q | ILE339 |
| Q | PRO340 |
| Q | GLN341 |
| Q | SER342 |
| Q | ILE343 |
| Q | SER344 |
| Q | GLU345 |
| E | HOH220 |
| E | HOH223 |
| E | HOH228 |
| E | HOH233 |
| Q | HOH995 |
| Q | HOH997 |
| Q | HOH1020 |
| Q | HOH1038 |
| Q | HOH1106 |
| site_id | VEF |
| Number of Residues | 29 |
| Details | SITE "VEF" IS THE VESTIGIAL SITE OF THE PROTOMER CONSISTING OF CHAINS F AND R. |
| Chain | Residue |
| F | TYR79 |
| F | VAL114 |
| F | ASN115 |
| F | ASN116 |
| F | ALA117 |
| F | ALA118 |
| F | MET122 |
| F | HIS125 |
| F | ASN127 |
| F | ARG142 |
| F | VAL157 |
| R | ASP304 |
| R | ARG307 |
| R | ILE339 |
| R | PRO340 |
| R | GLN341 |
| R | SER342 |
| R | ILE343 |
| R | SER344 |
| R | GLU345 |
| F | HOH1191 |
| R | HOH1199 |
| R | HOH1210 |
| F | HOH1217 |
| R | HOH1224 |
| F | HOH1226 |
| R | HOH1249 |
| F | HOH1267 |
| F | HOH1335 |
Functional Information from PROSITE/UniProt
| site_id | PS00083 |
| Number of Residues | 29 |
| Details | INTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. VaGrVvdqyGkpVpntlVEMwqanagGrY |
| Chain | Residue | Details |
| M | VAL380-TYR408 | |
| A | LEU51-TYR79 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7990141","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3pca |
| Chain | Residue | Details |
| M | TYR447 | |
| M | ARG457 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3pca |
| Chain | Residue | Details |
| N | TYR447 | |
| N | ARG457 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3pca |
| Chain | Residue | Details |
| O | TYR447 | |
| O | ARG457 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3pca |
| Chain | Residue | Details |
| P | TYR447 | |
| P | ARG457 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3pca |
| Chain | Residue | Details |
| Q | TYR447 | |
| Q | ARG457 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 3pca |
| Chain | Residue | Details |
| R | TYR447 | |
| R | ARG457 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| B | THR108 | metal ligand |
| B | ASP147 | metal ligand, proton shuttle (general acid/base) |
| B | VAL157 | electrostatic stabiliser |
| B | LEU160 | metal ligand |
| B | GLU162 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| D | THR108 | metal ligand |
| D | ASP147 | metal ligand, proton shuttle (general acid/base) |
| D | VAL157 | electrostatic stabiliser |
| D | LEU160 | metal ligand |
| D | GLU162 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| F | THR108 | metal ligand |
| F | ASP147 | metal ligand, proton shuttle (general acid/base) |
| F | VAL157 | electrostatic stabiliser |
| F | LEU160 | metal ligand |
| F | GLU162 | metal ligand |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| site_id | MCSA5 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| site_id | MCSA6 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
