7MGO
Crystal structure of F501H variant of 2-ketopropyl coenzyme M oxidoreductase/carboxylase (2-KPCC) from Xanthobacter autotrophicus
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 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 | 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 | HIS501 | 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 | HIS501 | electrostatic stabiliser |
