3PCB
STRUCTURE OF PROTOCATECHUATE 3,4-DIOXYGENASE COMPLEXED WITH 3-HYDROXYBENZOATE
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 | 5 |
| Details | BINDING SITE FOR RESIDUE FE M 600 |
| Chain | Residue |
| M | TYR408 |
| M | TYR447 |
| M | HIS460 |
| M | HIS462 |
| M | 3HB550 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE N 600 |
| Chain | Residue |
| N | TYR408 |
| N | TYR447 |
| N | HIS460 |
| N | HIS462 |
| N | 3HB550 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE O 600 |
| Chain | Residue |
| O | TYR408 |
| O | TYR447 |
| O | HIS460 |
| O | HIS462 |
| O | 3HB550 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE P 600 |
| Chain | Residue |
| P | TYR408 |
| P | TYR447 |
| P | HIS460 |
| P | HIS462 |
| P | 3HB550 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE Q 600 |
| Chain | Residue |
| Q | TYR408 |
| Q | TYR447 |
| Q | HIS460 |
| Q | HIS462 |
| Q | 3HB550 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE R 600 |
| Chain | Residue |
| R | TYR408 |
| R | TYR447 |
| R | HIS460 |
| R | HIS462 |
| R | 3HB550 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3HB M 550 |
| Chain | Residue |
| A | PRO15 |
| A | ARG133 |
| M | TYR324 |
| M | TYR447 |
| M | TRP449 |
| M | ARG457 |
| M | HIS462 |
| M | GLN477 |
| M | ILE491 |
| M | FE600 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 3HB M 551 |
| Chain | Residue |
| M | ARG333 |
| M | HOH676 |
| site_id | ACA |
| Number of Residues | 25 |
| Details | SITE "ACA" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS A AND M. |
| Chain | Residue |
| A | THR12 |
| M | TYR408 |
| M | TYR447 |
| M | TRP449 |
| M | ARG450 |
| M | ARG457 |
| M | HIS460 |
| M | HIS462 |
| M | GLN477 |
| M | ILE491 |
| M | FE600 |
| A | ALA13 |
| A | HOH203 |
| M | HOH624 |
| M | HOH631 |
| M | HOH632 |
| M | 3HB550 |
| M | HOH738 |
| A | GLY14 |
| A | PRO15 |
| A | TYR16 |
| A | ARG133 |
| A | GLY134 |
| M | TYR324 |
| M | THR326 |
| site_id | ACB |
| Number of Residues | 25 |
| 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 | TYR408 |
| N | TYR447 |
| N | TRP449 |
| N | ARG450 |
| N | ARG457 |
| N | HIS460 |
| N | HIS462 |
| N | GLN477 |
| N | ILE491 |
| N | FE600 |
| B | HOH242 |
| N | HOH630 |
| N | HOH637 |
| N | HOH638 |
| N | 3HB550 |
| N | HOH756 |
| site_id | ACC |
| Number of Residues | 25 |
| 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 | TYR408 |
| O | TYR447 |
| O | TRP449 |
| O | ARG450 |
| O | ARG457 |
| O | HIS460 |
| O | HIS462 |
| O | GLN477 |
| O | ILE491 |
| O | FE600 |
| C | HOH207 |
| O | HOH631 |
| O | HOH639 |
| O | HOH640 |
| O | 3HB550 |
| O | HOH755 |
| site_id | ACD |
| Number of Residues | 25 |
| Details | SITE "ACD" IS THE ACTIVE SITE OF THE PROTOMER CONSISTING OF CHAINS D AND P. |
| Chain | Residue |
| P | HOH748 |
| D | THR12 |
| D | ALA13 |
| D | GLY14 |
| D | PRO15 |
| D | TYR16 |
| D | ARG133 |
| D | GLY134 |
| P | TYR324 |
| P | THR326 |
| P | TYR408 |
| P | TYR447 |
| P | TRP449 |
| P | ARG450 |
| P | ARG457 |
| P | HIS460 |
| P | HIS462 |
| P | GLN477 |
| P | ILE491 |
| P | FE600 |
| D | HOH714 |
| P | HOH633 |
| P | HOH641 |
| P | HOH642 |
| P | 3HB550 |
| site_id | ACE |
| Number of Residues | 25 |
| 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 | TYR408 |
| Q | TYR447 |
| Q | TRP449 |
| Q | ARG450 |
| Q | ARG457 |
| Q | HIS460 |
| Q | HIS462 |
| Q | GLN477 |
| Q | ILE491 |
| Q | FE600 |
| E | HOH207 |
| Q | HOH987 |
| Q | HOH1002 |
| Q | HOH1003 |
| Q | 3HB550 |
| Q | HOH1177 |
| site_id | ACF |
| Number of Residues | 25 |
| 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 | TYR408 |
| R | TYR447 |
| R | TRP449 |
| R | ARG450 |
| R | ARG457 |
| R | HIS460 |
| R | HIS462 |
| R | GLN477 |
| R | ILE491 |
| R | FE600 |
| F | HOH1186 |
| R | HOH1223 |
| R | HOH1238 |
| R | HOH1239 |
| R | 3HB550 |
| R | HOH1413 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3HB N 550 |
| Chain | Residue |
| B | PRO15 |
| B | ARG133 |
| N | TYR324 |
| N | TYR447 |
| N | TRP449 |
| N | ARG457 |
| N | HIS462 |
| N | GLN477 |
| N | ILE491 |
| N | FE600 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 3HB N 551 |
| Chain | Residue |
| N | ARG333 |
| N | HOH687 |
| site_id | BC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 3HB O 550 |
| Chain | Residue |
| C | GLY14 |
| C | PRO15 |
| C | ARG133 |
| O | TYR324 |
| O | TYR447 |
| O | TRP449 |
| O | ARG457 |
| O | HIS462 |
| O | GLN477 |
| O | ILE491 |
| O | FE600 |
| site_id | BC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 3HB O 551 |
| Chain | Residue |
| O | ARG333 |
| O | HOH688 |
| site_id | BC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 3HB P 550 |
| Chain | Residue |
| D | GLY14 |
| D | PRO15 |
| D | ARG133 |
| P | TYR324 |
| P | TYR447 |
| P | TRP449 |
| P | ARG457 |
| P | HIS462 |
| P | GLN477 |
| P | ILE491 |
| P | FE600 |
| site_id | BC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE 3HB P 551 |
| Chain | Residue |
| P | ARG333 |
| P | HOH687 |
| R | PRO322 |
| site_id | CC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3HB Q 550 |
| Chain | Residue |
| E | PRO15 |
| E | ARG133 |
| Q | TYR324 |
| Q | TYR447 |
| Q | TRP449 |
| Q | ARG457 |
| Q | HIS462 |
| Q | GLN477 |
| Q | ILE491 |
| Q | FE600 |
| site_id | CC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 3HB Q 551 |
| Chain | Residue |
| Q | ARG333 |
| Q | HOH1074 |
| site_id | CC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3HB R 550 |
| Chain | Residue |
| F | PRO15 |
| F | ARG133 |
| R | TYR324 |
| R | TYR447 |
| R | TRP449 |
| R | ARG457 |
| R | HIS462 |
| R | GLN477 |
| R | ILE491 |
| R | FE600 |
| site_id | CC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE 3HB R 551 |
| Chain | Residue |
| R | ARG333 |
| R | HOH1310 |
| 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 | HOH219 |
| A | HOH222 |
| M | HOH636 |
| A | HOH231 |
| M | HOH642 |
| A | HOH234 |
| M | HOH657 |
| A | HOH247 |
| M | HOH714 |
| 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 | HOH282 |
| B | HOH290 |
| N | HOH643 |
| B | HOH308 |
| N | HOH651 |
| B | HOH317 |
| N | HOH666 |
| B | HOH359 |
| N | HOH727 |
| 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 | HOH220 |
| C | HOH223 |
| O | HOH644 |
| C | HOH231 |
| O | HOH652 |
| C | HOH234 |
| O | HOH668 |
| C | HOH246 |
| C | HOH267 |
| 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 | HOH754 |
| P | HOH639 |
| D | HOH773 |
| D | HOH780 |
| P | HOH652 |
| D | HOH789 |
| P | HOH668 |
| D | HOH831 |
| P | HOH723 |
| 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 | HOH222 |
| Q | HOH998 |
| E | HOH229 |
| E | HOH234 |
| Q | HOH1023 |
| E | HOH237 |
| Q | HOH1049 |
| E | HOH249 |
| Q | HOH1135 |
| 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 | HOH1226 |
| F | HOH1234 |
| R | HOH1245 |
| F | HOH1252 |
| R | HOH1259 |
| F | HOH1261 |
| R | HOH1285 |
| F | HOH1303 |
| R | HOH1371 |
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 | 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 | ALA151 | metal ligand, proton shuttle (general acid/base) |
| B | ILE161 | electrostatic stabiliser |
| B | PRO164 | metal ligand |
| B | ARG166 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| D | THR108 | metal ligand |
| D | ALA151 | metal ligand, proton shuttle (general acid/base) |
| D | ILE161 | electrostatic stabiliser |
| D | PRO164 | metal ligand |
| D | ARG166 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| F | THR108 | metal ligand |
| F | ALA151 | metal ligand, proton shuttle (general acid/base) |
| F | ILE161 | electrostatic stabiliser |
| F | PRO164 | metal ligand |
| F | ARG166 | 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 |
