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. LlGqVydgnGhlVrdsfLEVwqadanGeY |
Chain | Residue | Details |
A | LEU51-TYR79 | |
M | VAL380-TYR408 |
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 |