1MOK
NADPH DEPENDENT 2-KETOPROPYL COENZYME M OXIDOREDUCTASE/CARBOXYLASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042208 | biological_process | propylene catabolic process |
| A | 0050628 | molecular_function | 2-oxopropyl-CoM reductase (carboxylating) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042208 | biological_process | propylene catabolic process |
| B | 0050628 | molecular_function | 2-oxopropyl-CoM reductase (carboxylating) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0042208 | biological_process | propylene catabolic process |
| C | 0050628 | molecular_function | 2-oxopropyl-CoM reductase (carboxylating) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0042208 | biological_process | propylene catabolic process |
| D | 0050628 | molecular_function | 2-oxopropyl-CoM reductase (carboxylating) activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD A 524 |
| Chain | Residue |
| A | GLY50 |
| A | ALA86 |
| A | CYS87 |
| A | HIS90 |
| A | HIS91 |
| A | PRO157 |
| A | ALA158 |
| A | ALA181 |
| A | VAL182 |
| A | HIS202 |
| A | THR225 |
| A | GLY52 |
| A | TYR229 |
| A | GLY352 |
| A | ASP353 |
| A | MET359 |
| A | GLU360 |
| A | MET361 |
| A | ALA364 |
| A | PHE390 |
| B | PHE501 |
| A | ALA53 |
| A | ALA54 |
| A | ASP73 |
| A | ARG74 |
| A | TRP75 |
| A | GLY80 |
| A | SER81 |
| site_id | AC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE FAD B 524 |
| Chain | Residue |
| A | PHE501 |
| B | GLY50 |
| B | GLY51 |
| B | ALA53 |
| B | ALA54 |
| B | ASP73 |
| B | ARG74 |
| B | TRP75 |
| B | GLY80 |
| B | SER81 |
| B | ALA86 |
| B | CYS87 |
| B | HIS90 |
| B | HIS91 |
| B | PRO157 |
| B | ALA158 |
| B | ALA181 |
| B | VAL182 |
| B | GLY183 |
| B | HIS202 |
| B | THR225 |
| B | GLU314 |
| B | GLY352 |
| B | ASP353 |
| B | MET359 |
| B | GLU360 |
| B | MET361 |
| B | ALA364 |
| site_id | AC3 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE FAD C 524 |
| Chain | Residue |
| C | GLY50 |
| C | ALA53 |
| C | ALA54 |
| C | ASP73 |
| C | ARG74 |
| C | TRP75 |
| C | GLY80 |
| C | SER81 |
| C | ALA86 |
| C | CYS87 |
| C | HIS90 |
| C | HIS91 |
| C | PRO157 |
| C | ALA158 |
| C | ALA181 |
| C | VAL182 |
| C | GLY183 |
| C | HIS202 |
| C | THR225 |
| C | TYR229 |
| C | GLY352 |
| C | ASP353 |
| C | MET359 |
| C | GLU360 |
| C | MET361 |
| D | PHE501 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE FAD D 524 |
| Chain | Residue |
| D | ALA181 |
| D | VAL182 |
| D | HIS202 |
| D | THR225 |
| D | TYR229 |
| D | GLY352 |
| D | ASP353 |
| D | MET359 |
| D | GLU360 |
| D | MET361 |
| D | ALA364 |
| D | PHE390 |
| C | PHE501 |
| D | GLY50 |
| D | GLY52 |
| D | ALA53 |
| D | ALA54 |
| D | VAL72 |
| D | ASP73 |
| D | ARG74 |
| D | TRP75 |
| D | GLY80 |
| D | SER81 |
| D | ALA86 |
| D | CYS87 |
| D | HIS90 |
| D | HIS91 |
| D | PRO157 |
| D | ALA158 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12390015","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16388586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21192936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1MO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MOK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2C3C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2C3D","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q6J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"12390015","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21192936","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16388586","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1MO9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q6J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21192936","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16388586","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3Q6J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16388586","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21192936","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2C3C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3Q6J","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12390015 |
| Chain | Residue | Details |
| A | CYS87 | |
| A | CYS82 | |
| A | HIS137 | |
| A | LEU78 | |
| A | PHE501 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12390015 |
| Chain | Residue | Details |
| B | CYS87 | |
| B | HIS137 | |
| B | CYS82 | |
| B | LEU78 | |
| B | PHE501 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12390015 |
| Chain | Residue | Details |
| C | CYS87 | |
| C | HIS137 | |
| C | CYS82 | |
| C | LEU78 | |
| C | PHE501 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | a catalytic site defined by CSA, PubMed 12390015 |
| Chain | Residue | Details |
| D | CYS87 | |
| D | HIS137 | |
| D | CYS82 | |
| D | LEU78 | |
| D | PHE501 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 378 |
| Chain | Residue | Details |
| A | LEU78 | electrostatic stabiliser, modifies pKa |
| A | CYS82 | covalent catalysis |
| A | CYS87 | covalent catalysis |
| A | HIS137 | modifies pKa |
| A | PHE501 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 5 |
| Details | M-CSA 378 |
| Chain | Residue | Details |
| B | LEU78 | electrostatic stabiliser, modifies pKa |
| B | CYS82 | covalent catalysis |
| B | CYS87 | covalent catalysis |
| B | HIS137 | modifies pKa |
| B | PHE501 | electrostatic stabiliser |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 378 |
| Chain | Residue | Details |
| C | LEU78 | electrostatic stabiliser, modifies pKa |
| C | CYS82 | covalent catalysis |
| C | CYS87 | covalent catalysis |
| C | HIS137 | modifies pKa |
| C | PHE501 | electrostatic stabiliser |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 378 |
| Chain | Residue | Details |
| D | LEU78 | electrostatic stabiliser, modifies pKa |
| D | CYS82 | covalent catalysis |
| D | CYS87 | covalent catalysis |
| D | HIS137 | modifies pKa |
| D | PHE501 | electrostatic stabiliser |






