4WHS
4-fluorocatechol bound to Protocatechuate 3,4-dioxygenase (pseudomonas putida) at pH 8.5
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 | 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 | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| B | 0042952 | biological_process | beta-ketoadipate pathway |
| B | 0046872 | molecular_function | metal ion binding |
| 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 | 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 | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| D | 0042952 | biological_process | beta-ketoadipate pathway |
| D | 0046872 | molecular_function | metal ion binding |
| 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 | 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 | 0019619 | biological_process | 3,4-dihydroxybenzoate catabolic process |
| F | 0042952 | biological_process | beta-ketoadipate pathway |
| F | 0046872 | molecular_function | metal ion binding |
| F | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | binding site for residue 3N8 A 301 |
| Chain | Residue |
| A | PRO164 |
| A | ARG167 |
| A | GLU168 |
| A | ILE171 |
| A | HOH470 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 302 |
| Chain | Residue |
| A | ASN37 |
| A | THR105 |
| A | HIS107 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue FE F 601 |
| Chain | Residue |
| F | TYR447 |
| F | HIS460 |
| F | HIS462 |
| F | 3N8605 |
| F | TYR408 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | binding site for residue 3N8 F 602 |
| Chain | Residue |
| D | ARG450 |
| D | PRO453 |
| D | MET516 |
| D | HOH762 |
| F | SER338 |
| F | HOH793 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue BME F 603 |
| Chain | Residue |
| A | HOH413 |
| A | HOH558 |
| F | MET488 |
| F | MET510 |
| F | HOH736 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue 3N8 F 604 |
| Chain | Residue |
| A | LEU160 |
| B | SER338 |
| B | PRO340 |
| F | ARG450 |
| F | PRO453 |
| F | MET516 |
| F | HOH931 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue 3N8 F 605 |
| Chain | Residue |
| E | PRO15 |
| E | TYR16 |
| E | HOH534 |
| F | TYR408 |
| F | TYR447 |
| F | TRP449 |
| F | ARG457 |
| F | HIS460 |
| F | HIS462 |
| F | FE601 |
| F | HOH763 |
| F | HOH889 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue CL F 606 |
| Chain | Residue |
| F | PRO418 |
| F | LEU419 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | binding site for residue 3N8 E 301 |
| Chain | Residue |
| E | PRO164 |
| E | ARG167 |
| E | GLU168 |
| E | ILE171 |
| E | HOH488 |
| site_id | AD1 |
| Number of Residues | 7 |
| Details | binding site for residue MUC E 302 |
| Chain | Residue |
| E | GLU168 |
| E | THR169 |
| E | ILE171 |
| E | ARG184 |
| E | PHE185 |
| E | ASP186 |
| E | ARG188 |
| site_id | AD2 |
| Number of Residues | 5 |
| Details | binding site for residue 3N8 C 301 |
| Chain | Residue |
| C | PRO164 |
| C | ARG167 |
| C | GLU168 |
| C | ILE171 |
| C | HOH449 |
| site_id | AD3 |
| Number of Residues | 5 |
| Details | binding site for residue BME C 302 |
| Chain | Residue |
| C | ALA151 |
| C | HOH473 |
| C | HOH488 |
| C | HOH549 |
| C | HOH561 |
| site_id | AD4 |
| Number of Residues | 6 |
| Details | binding site for residue BME C 303 |
| Chain | Residue |
| B | 3N8604 |
| C | ASN116 |
| C | HOH439 |
| C | HOH509 |
| C | HOH532 |
| D | PRO340 |
| site_id | AD5 |
| Number of Residues | 8 |
| Details | binding site for residue MUC C 304 |
| Chain | Residue |
| C | GLU168 |
| C | THR169 |
| C | ILE171 |
| C | ALA172 |
| C | ARG184 |
| C | PHE185 |
| C | ASP186 |
| C | HOH527 |
| site_id | AD6 |
| Number of Residues | 5 |
| Details | binding site for residue FE D 601 |
| Chain | Residue |
| D | TYR408 |
| D | TYR447 |
| D | HIS460 |
| D | HIS462 |
| D | 3N8602 |
| site_id | AD7 |
| Number of Residues | 12 |
| Details | binding site for residue 3N8 D 602 |
| Chain | Residue |
| C | PRO15 |
| C | TYR16 |
| C | HOH554 |
| D | TYR408 |
| D | TYR447 |
| D | TRP449 |
| D | ARG457 |
| D | HIS460 |
| D | HIS462 |
| D | FE601 |
| D | HOH891 |
| D | HOH914 |
| site_id | AD8 |
| Number of Residues | 3 |
| Details | binding site for residue 3N8 D 603 |
| Chain | Residue |
| D | ARG333 |
| D | HOH907 |
| B | ILE328 |
| site_id | AD9 |
| Number of Residues | 5 |
| Details | binding site for residue FE B 601 |
| Chain | Residue |
| B | TYR408 |
| B | TYR447 |
| B | HIS460 |
| B | HIS462 |
| B | 3N8603 |
| site_id | AE1 |
| Number of Residues | 8 |
| Details | binding site for residue BME B 602 |
| Chain | Residue |
| B | MET488 |
| B | MET510 |
| B | HOH713 |
| B | HOH718 |
| B | HOH740 |
| C | PRO1 |
| C | ILE2 |
| C | GLU3 |
| site_id | AE2 |
| Number of Residues | 14 |
| Details | binding site for residue 3N8 B 603 |
| Chain | Residue |
| A | PRO15 |
| A | TYR16 |
| A | HOH556 |
| B | TYR408 |
| B | TYR447 |
| B | TRP449 |
| B | ARG457 |
| B | HIS460 |
| B | HIS462 |
| B | FE601 |
| B | HOH878 |
| B | HOH905 |
| B | HOH915 |
| B | HOH929 |
| site_id | AE3 |
| Number of Residues | 7 |
| Details | binding site for residue 3N8 B 604 |
| Chain | Residue |
| B | ARG450 |
| B | PRO453 |
| B | MET516 |
| B | HOH719 |
| C | LEU160 |
| C | BME303 |
| D | SER338 |
| site_id | AE4 |
| Number of Residues | 2 |
| Details | binding site for residue CL B 605 |
| Chain | Residue |
| B | ARG409 |
| B | HIS410 |
| site_id | AE5 |
| Number of Residues | 4 |
| Details | binding site for residue CL B 606 |
| Chain | Residue |
| B | TRP449 |
| B | ARG450 |
| B | HOH881 |
| B | HOH915 |
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 | |
| D | VAL380-TYR408 | |
| F | VAL380-TYR408 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"7990141","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| E | THR108 | metal ligand |
| E | ALA151 | metal ligand, proton shuttle (general acid/base) |
| E | ILE161 | electrostatic stabiliser |
| E | PRO164 | metal ligand |
| E | ARG166 | metal ligand |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 936 |
| Chain | Residue | Details |
| F | TYR408 | metal ligand |
| F | TYR447 | metal ligand, proton shuttle (general acid/base) |
| F | ARG457 | electrostatic stabiliser |
| F | HIS460 | metal ligand |
| F | HIS462 | metal ligand |
