3T63
Axial Ligand Swapping In Double Mutant Maintains Intradiol-cleavage Chemistry in Protocatechuate 3,4-Dioxygenase
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 |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME A 201 |
| Chain | Residue |
| A | TYR56 |
| A | ASP57 |
| A | GLY60 |
| A | ARG188 |
| A | ILE189 |
| A | GLN190 |
| A | GLY191 |
| A | GLU192 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | THR169 |
| A | LEU170 |
| A | ILE171 |
| A | ARG184 |
| A | PHE185 |
| A | ASP186 |
| A | ARG188 |
| A | HOH955 |
| A | GLU168 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 203 |
| Chain | Residue |
| A | ASN37 |
| A | THR105 |
| A | HIS107 |
| A | HOH682 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL B 201 |
| Chain | Residue |
| B | GLU168 |
| B | THR169 |
| B | ILE171 |
| B | ARG184 |
| B | PHE185 |
| B | ASP186 |
| B | ARG188 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 202 |
| Chain | Residue |
| B | ASN37 |
| B | ARG38 |
| B | THR105 |
| B | HIS107 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 201 |
| Chain | Residue |
| C | THR169 |
| C | ILE171 |
| C | ARG184 |
| C | PHE185 |
| C | ASP186 |
| C | ARG188 |
| C | HOH954 |
| C | HOH1492 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 202 |
| Chain | Residue |
| C | ASN37 |
| C | THR105 |
| C | HIS107 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME M 1 |
| Chain | Residue |
| M | TYR408 |
| M | ARG457 |
| M | HIS460 |
| M | TYR462 |
| M | BME542 |
| M | FE600 |
| M | HOH613 |
| M | HOH1559 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BME M 539 |
| Chain | Residue |
| M | PHE356 |
| M | CYS429 |
| M | LEU430 |
| M | HOH568 |
| site_id | BC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME M 540 |
| Chain | Residue |
| M | ARG450 |
| M | PRO453 |
| M | HOH1460 |
| M | HOH1545 |
| N | HOH145 |
| N | SER338 |
| N | ILE339 |
| N | PRO340 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL M 541 |
| Chain | Residue |
| M | GLN503 |
| M | ILE505 |
| M | ARG522 |
| M | PHE523 |
| M | ASP524 |
| site_id | BC3 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE SO4 M 7 |
| Chain | Residue |
| M | ARG383 |
| site_id | BC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BME M 542 |
| Chain | Residue |
| A | PRO15 |
| A | ARG133 |
| A | HOH1482 |
| M | BME1 |
| M | HOH296 |
| M | TYR324 |
| M | THR326 |
| M | TRP449 |
| M | HOH1488 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME M 543 |
| Chain | Residue |
| A | PHE200 |
| M | ILE310 |
| M | ILE339 |
| M | PRO340 |
| M | GLN341 |
| M | HOH547 |
| O | PRO453 |
| O | PRO515 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE M 600 |
| Chain | Residue |
| M | BME1 |
| M | TYR408 |
| M | HIS460 |
| M | TYR462 |
| M | HOH1559 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME N 1 |
| Chain | Residue |
| B | TYR16 |
| N | TYR408 |
| N | ARG457 |
| N | TYR462 |
| N | BME540 |
| N | HOH577 |
| N | FE600 |
| N | HOH1560 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME N 539 |
| Chain | Residue |
| N | PHE356 |
| N | CYS429 |
| N | LEU430 |
| N | HOH700 |
| N | HOH1102 |
| site_id | BC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE BME N 540 |
| Chain | Residue |
| B | PRO15 |
| B | ARG133 |
| N | BME1 |
| N | HOH65 |
| N | TYR324 |
| N | THR326 |
| N | TRP449 |
| N | HOH1484 |
| N | HOH1536 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE N 600 |
| Chain | Residue |
| N | BME1 |
| N | TYR408 |
| N | HIS460 |
| N | TYR462 |
| N | HOH1560 |
| site_id | CC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE BME O 1 |
| Chain | Residue |
| C | TYR16 |
| O | TYR408 |
| O | TRP449 |
| O | ARG457 |
| O | HIS460 |
| O | TYR462 |
| O | BME539 |
| O | BME540 |
| O | FE600 |
| O | HOH654 |
| O | HOH1561 |
| O | HOH1566 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BME O 539 |
| Chain | Residue |
| C | PRO15 |
| O | BME1 |
| O | TRP449 |
| O | ARG450 |
| O | BME540 |
| O | HOH1566 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BME O 540 |
| Chain | Residue |
| C | PRO15 |
| C | ARG133 |
| O | BME1 |
| O | HOH143 |
| O | TYR324 |
| O | THR326 |
| O | TRP449 |
| O | BME539 |
| site_id | CC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE O 600 |
| Chain | Residue |
| O | BME1 |
| O | TYR408 |
| O | HIS460 |
| O | TYR462 |
| O | HOH1561 |
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 | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:7990141 |
| Chain | Residue | Details |
| M | TYR408 | |
| O | ALA447 | |
| O | HIS460 | |
| O | TYR462 | |
| M | ALA447 | |
| M | HIS460 | |
| M | TYR462 | |
| N | TYR408 | |
| N | ALA447 | |
| N | HIS460 | |
| N | TYR462 | |
| 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 | ALA447 | metal ligand, proton shuttle (general acid/base) |
| M | ARG457 | electrostatic stabiliser |
| M | HIS460 | metal ligand |
| M | TYR462 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| N | TYR408 | metal ligand |
| N | ALA447 | metal ligand, proton shuttle (general acid/base) |
| N | ARG457 | electrostatic stabiliser |
| N | HIS460 | metal ligand |
| N | TYR462 | metal ligand |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| O | TYR408 | metal ligand |
| O | ALA447 | metal ligand, proton shuttle (general acid/base) |
| O | ARG457 | electrostatic stabiliser |
| O | HIS460 | metal ligand |
| O | TYR462 | metal ligand |
