2C3C
2.01 Angstrom X-ray crystal structure of a mixed disulfide between coenzyme M and NADPH-dependent oxidoreductase 2-ketopropyl coenzyme M 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE COM A1000 |
| Chain | Residue |
| A | ALA53 |
| A | HOH2088 |
| B | ACN1525 |
| A | ARG56 |
| A | PHE57 |
| A | GLY79 |
| A | CYS82 |
| A | PRO83 |
| A | MET140 |
| A | MET361 |
| A | ARG365 |
| site_id | AC2 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD A1524 |
| Chain | Residue |
| A | GLY50 |
| A | GLY52 |
| A | ALA53 |
| A | ALA54 |
| A | ASP73 |
| A | ARG74 |
| A | TRP75 |
| A | GLY80 |
| A | SER81 |
| A | ALA86 |
| A | CYS87 |
| A | HIS90 |
| A | HIS91 |
| A | PRO157 |
| A | ALA158 |
| A | ALA181 |
| A | VAL182 |
| A | GLY183 |
| A | HIS202 |
| A | TYR229 |
| A | GLY352 |
| A | ASP353 |
| A | MET359 |
| A | GLU360 |
| A | MET361 |
| A | ALA364 |
| A | NAP1526 |
| A | HOH2050 |
| A | HOH2055 |
| A | HOH2102 |
| A | HOH2252 |
| A | HOH2253 |
| A | HOH2258 |
| A | HOH2364 |
| A | HOH2365 |
| A | HOH2366 |
| B | PHE501 |
| site_id | AC3 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE NAP A1526 |
| Chain | Residue |
| A | LEU189 |
| A | GLY222 |
| A | SER223 |
| A | LYS224 |
| A | THR225 |
| A | GLU228 |
| A | ARG245 |
| A | THR246 |
| A | LYS250 |
| A | LEU312 |
| A | GLY313 |
| A | MET359 |
| A | GLU360 |
| A | FAD1524 |
| A | HOH2368 |
| A | HOH2369 |
| A | HOH2370 |
| A | HOH2371 |
| A | HOH2372 |
| A | HOH2373 |
| A | HOH2374 |
| A | HOH2375 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE COM B1000 |
| Chain | Residue |
| A | ACN1525 |
| A | HOH2367 |
| B | ALA53 |
| B | ARG56 |
| B | PHE57 |
| B | GLY79 |
| B | CYS82 |
| B | PRO83 |
| B | MET140 |
| B | MET361 |
| B | ARG365 |
| site_id | AC5 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD B1524 |
| Chain | Residue |
| B | VAL182 |
| B | GLY183 |
| B | HIS202 |
| B | TYR229 |
| B | GLY352 |
| B | ASP353 |
| B | MET359 |
| B | GLU360 |
| B | MET361 |
| B | ALA364 |
| B | NAP1526 |
| B | HOH2035 |
| B | HOH2326 |
| B | HOH2327 |
| B | HOH2328 |
| B | HOH2329 |
| B | HOH2330 |
| A | PHE501 |
| B | GLY50 |
| B | GLY52 |
| B | ALA53 |
| B | ALA54 |
| B | VAL72 |
| B | ASP73 |
| B | ARG74 |
| B | TRP75 |
| B | GLY80 |
| B | SER81 |
| B | ALA86 |
| B | CYS87 |
| B | HIS90 |
| B | HIS91 |
| B | PRO157 |
| B | ALA158 |
| B | ALA181 |
| site_id | AC6 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE NAP B1526 |
| Chain | Residue |
| B | HIS90 |
| B | LEU189 |
| B | GLY222 |
| B | SER223 |
| B | LYS224 |
| B | THR225 |
| B | GLU228 |
| B | ARG245 |
| B | THR246 |
| B | LYS250 |
| B | GLY311 |
| B | LEU312 |
| B | GLY313 |
| B | MET359 |
| B | GLU360 |
| B | PHE390 |
| B | FAD1524 |
| B | HOH2122 |
| B | HOH2187 |
| B | HOH2332 |
| B | HOH2333 |
| B | HOH2334 |
| B | HOH2335 |
| B | HOH2336 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ACN A1525 |
| Chain | Residue |
| A | PHE501 |
| A | HIS506 |
| A | GLN509 |
| A | HOH2367 |
| B | ARG365 |
| B | COM1000 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ACN B1525 |
| Chain | Residue |
| A | ARG365 |
| A | COM1000 |
| A | HOH2088 |
| B | LEU431 |
| B | PHE501 |
| B | HIS506 |
| B | GLN509 |
| B | HOH2331 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| 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 | 4 |
| 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 | 2 |
| 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 | 10 |
| 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 | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS87 | |
| A | CYS82 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS87 | |
| B | CYS82 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS87 | |
| A | HIS137 | |
| A | CYS82 | |
| A | LEU78 | |
| A | PHE501 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS87 | |
| B | HIS137 | |
| B | CYS82 | |
| B | LEU78 | |
| B | 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 |
