3MFL
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 | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 201 |
| Chain | Residue |
| A | ASN37 |
| A | THR105 |
| A | HIS107 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | HOH901 |
| A | THR169 |
| A | ILE171 |
| A | ARG184 |
| A | PHE185 |
| A | ASP186 |
| A | ARG188 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 203 |
| Chain | Residue |
| A | ARG38 |
| A | LEU39 |
| A | LYS41 |
| A | LEU85 |
| A | ASN87 |
| A | ALA88 |
| A | ASN90 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME A 204 |
| Chain | Residue |
| A | PRO164 |
| A | HOH255 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE M 600 |
| Chain | Residue |
| M | TYR408 |
| M | HIS447 |
| M | HIS460 |
| M | TYR462 |
| M | DHY539 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CO3 M 1 |
| Chain | Residue |
| M | ARG383 |
| site_id | AC7 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DHY M 539 |
| Chain | Residue |
| A | PRO15 |
| A | TYR16 |
| A | ARG133 |
| A | HOH232 |
| M | TYR408 |
| M | HIS447 |
| M | PRO448 |
| M | TRP449 |
| M | ARG457 |
| M | HIS460 |
| M | TYR462 |
| M | HOH579 |
| M | FE600 |
| M | HOH808 |
| M | HOH907 |
| M | HOH916 |
| site_id | AC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 201 |
| Chain | Residue |
| B | ASN37 |
| B | ARG38 |
| B | THR105 |
| B | HIS107 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 202 |
| Chain | Residue |
| B | GLU168 |
| B | THR169 |
| B | ILE171 |
| B | ARG184 |
| B | PHE185 |
| B | ASP186 |
| B | ARG188 |
| B | HOH883 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME B 203 |
| Chain | Residue |
| B | LEU23 |
| B | ASN28 |
| B | PRO29 |
| B | HOH742 |
| N | PHE367 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BME B 204 |
| Chain | Residue |
| B | GLU69 |
| B | ASN127 |
| B | ILE128 |
| B | SER129 |
| B | HIS140 |
| B | HOH249 |
| N | ILE470 |
| site_id | BC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE N 600 |
| Chain | Residue |
| N | TYR408 |
| N | HIS447 |
| N | HIS460 |
| N | TYR462 |
| N | DHY539 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 N 4 |
| Chain | Residue |
| N | ARG383 |
| N | ASP434 |
| N | HOH723 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL N 1 |
| Chain | Residue |
| N | GLN503 |
| N | ILE505 |
| N | ARG522 |
| N | PHE523 |
| N | ASP524 |
| site_id | BC6 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE DHY N 539 |
| Chain | Residue |
| B | PRO15 |
| B | TYR16 |
| B | HOH894 |
| N | TYR408 |
| N | HIS447 |
| N | TRP449 |
| N | ARG450 |
| N | ARG457 |
| N | HIS460 |
| N | TYR462 |
| N | FE600 |
| N | HOH756 |
| N | HOH897 |
| N | HOH917 |
| N | HOH1023 |
| N | HOH1037 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 201 |
| Chain | Residue |
| C | ASN37 |
| C | THR105 |
| C | HIS107 |
| C | HOH990 |
| site_id | BC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 202 |
| Chain | Residue |
| C | ILE171 |
| C | ARG184 |
| C | PHE185 |
| C | ASP186 |
| C | ARG188 |
| C | HOH955 |
| C | HOH1048 |
| C | THR169 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE O 600 |
| Chain | Residue |
| O | TYR408 |
| O | HIS447 |
| O | HIS460 |
| O | TYR462 |
| O | DHY540 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL O 1 |
| Chain | Residue |
| O | GLN503 |
| O | ILE505 |
| O | LYS507 |
| O | ARG522 |
| O | PHE523 |
| O | ASP524 |
| site_id | CC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE DHY O 540 |
| Chain | Residue |
| C | PRO15 |
| C | TYR16 |
| O | TYR408 |
| O | HIS447 |
| O | TRP449 |
| O | ARG450 |
| O | ARG457 |
| O | HIS460 |
| O | TYR462 |
| O | FE600 |
| O | HOH768 |
| O | HOH770 |
| O | HOH887 |
| O | HOH914 |
| O | HOH1022 |
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 | HIS447 | |
| O | HIS460 | |
| O | TYR462 | |
| M | HIS447 | |
| M | HIS460 | |
| M | TYR462 | |
| N | TYR408 | |
| N | HIS447 | |
| 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 | HIS447 | 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 | HIS447 | 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 | HIS447 | metal ligand, proton shuttle (general acid/base) |
| O | ARG457 | electrostatic stabiliser |
| O | HIS460 | metal ligand |
| O | TYR462 | metal ligand |
