3MI1
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 | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 201 |
| Chain | Residue |
| A | ASN37 |
| A | THR105 |
| A | HIS107 |
| A | HOH258 |
| A | HOH631 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 202 |
| Chain | Residue |
| A | ASP186 |
| A | ARG188 |
| A | HOH235 |
| A | HOH885 |
| A | HOH1033 |
| A | THR169 |
| A | ILE171 |
| A | ARG184 |
| A | PHE185 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE M 600 |
| Chain | Residue |
| A | THR12 |
| A | GLY14 |
| A | HOH1055 |
| M | ARG457 |
| M | TYR462 |
| M | GLN477 |
| M | HOH1067 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 203 |
| Chain | Residue |
| A | ARG133 |
| A | HOH1055 |
| A | HOH1084 |
| A | HOH1163 |
| M | TYR324 |
| M | THR326 |
| M | TRP449 |
| M | HOH552 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL M 1 |
| Chain | Residue |
| B | ILE2 |
| M | GLN503 |
| M | LYS507 |
| M | ARG522 |
| M | PHE523 |
| M | ASP524 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME M 541 |
| Chain | Residue |
| M | ARG409 |
| M | PRO421 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME M 542 |
| Chain | Residue |
| M | PHE535 |
| O | HIS361 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 201 |
| Chain | Residue |
| B | ASN37 |
| B | ARG38 |
| B | THR105 |
| B | HIS107 |
| B | HOH450 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 202 |
| Chain | Residue |
| B | ARG133 |
| B | HOH557 |
| B | HOH1060 |
| N | HOH226 |
| N | TYR324 |
| N | THR326 |
| N | TRP449 |
| N | HOH1198 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE N 600 |
| Chain | Residue |
| B | THR12 |
| B | GLY14 |
| B | HOH1060 |
| N | ARG457 |
| N | TYR462 |
| N | GLN477 |
| N | HOH1077 |
| site_id | BC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 N 8 |
| Chain | Residue |
| N | ARG414 |
| N | ARG450 |
| N | HOH1219 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL N 539 |
| Chain | Residue |
| N | GLN503 |
| N | ILE505 |
| N | LYS507 |
| N | ARG522 |
| N | PHE523 |
| N | ASP524 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME N 540 |
| Chain | Residue |
| N | ARG407 |
| N | LEU419 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 C 201 |
| Chain | Residue |
| C | ASN37 |
| C | THR105 |
| C | HIS107 |
| C | HOH669 |
| site_id | BC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 C 202 |
| Chain | Residue |
| C | ARG133 |
| C | HOH665 |
| C | HOH1058 |
| C | HOH1242 |
| O | HOH236 |
| O | TYR324 |
| O | THR326 |
| O | TRP449 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL C 203 |
| Chain | Residue |
| C | THR169 |
| C | ILE171 |
| C | ARG184 |
| C | PHE185 |
| C | ASP186 |
| C | ARG188 |
| C | HOH673 |
| C | HOH1028 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME C 204 |
| Chain | Residue |
| C | PRO164 |
| C | ARG167 |
| C | HOH679 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME C 205 |
| Chain | Residue |
| C | LEU23 |
| C | ASN28 |
| C | PRO29 |
| C | HOH530 |
| O | PHE367 |
| site_id | CC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FE O 600 |
| Chain | Residue |
| C | GLY14 |
| C | HOH1058 |
| O | ARG457 |
| O | TYR462 |
| O | GLN477 |
| O | HOH1078 |
| C | THR12 |
| site_id | CC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL O 1 |
| Chain | Residue |
| O | GLN503 |
| O | ILE505 |
| O | ARG522 |
| O | PHE523 |
| O | ASP524 |
| site_id | CC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME O 539 |
| Chain | Residue |
| O | ARG407 |
| O | LEU419 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BME O 540 |
| Chain | Residue |
| O | THR321 |
| O | PRO322 |
| O | ASP323 |
| O | LYS493 |
| O | HOH551 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL O 541 |
| Chain | Residue |
| O | ARG383 |
| site_id | CC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 203 |
| Chain | Residue |
| B | GLU168 |
| B | THR169 |
| B | ILE171 |
| B | ARG184 |
| B | PHE185 |
| B | ASP186 |
| B | ARG188 |
| B | HOH564 |
| B | HOH973 |
| site_id | CC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 O 3 |
| Chain | Residue |
| O | ASN412 |
| O | ARG414 |
| O | ARG450 |
| site_id | CC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL M 540 |
| Chain | Residue |
| M | HOH87 |
| M | ARG407 |
| M | LEU419 |
| site_id | CC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE BME N 1 |
| Chain | Residue |
| N | HIS534 |
| N | PHE535 |
| N | GLU536 |
| site_id | DC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE BME O 542 |
| Chain | Residue |
| O | HIS534 |
| O | PHE535 |
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 | TYR447 | |
| O | HIS460 | |
| O | TYR462 | |
| M | TYR447 | |
| M | HIS460 | |
| M | TYR462 | |
| N | TYR408 | |
| N | TYR447 | |
| 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 | TYR447 | 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 | TYR447 | 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 | TYR447 | metal ligand, proton shuttle (general acid/base) |
| O | ARG457 | electrostatic stabiliser |
| O | HIS460 | metal ligand |
| O | TYR462 | metal ligand |
