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 | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0042208 | biological_process | propylene catabolic process |
| A | 0050628 | molecular_function | 2-oxopropyl-CoM reductase (carboxylating) activity |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0003955 | molecular_function | NAD(P)H dehydrogenase (quinone) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0042208 | biological_process | propylene catabolic process |
| B | 0050628 | molecular_function | 2-oxopropyl-CoM reductase (carboxylating) activity |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12390015, ECO:0000269|PubMed:16388586, ECO:0000269|PubMed:21192936, ECO:0007744|PDB:1MO9, ECO:0007744|PDB:1MOK, ECO:0007744|PDB:2C3C, ECO:0007744|PDB:2C3D, ECO:0007744|PDB:3Q6J |
| Chain | Residue | Details |
| A | ALA158 | |
| A | ASP353 | |
| A | MET361 | |
| A | HIS501 | |
| B | ALA53 | |
| B | SER81 | |
| B | ALA158 | |
| B | ASP353 | |
| B | MET361 | |
| B | HIS501 | |
| A | ALA53 | |
| A | SER81 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:12390015, ECO:0000269|PubMed:21192936, ECO:0000305|PubMed:16388586, ECO:0007744|PDB:1MO9, ECO:0007744|PDB:3Q6J |
| Chain | Residue | Details |
| A | ARG56 | |
| A | ARG365 | |
| B | ARG56 | |
| B | ARG365 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:21192936, ECO:0000305|PubMed:16388586, ECO:0007744|PDB:3Q6J |
| Chain | Residue | Details |
| A | CYS82 | |
| B | CYS82 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16388586, ECO:0000269|PubMed:21192936, ECO:0007744|PDB:2C3C, ECO:0007744|PDB:3Q6J |
| Chain | Residue | Details |
| A | GLY222 | |
| A | ARG245 | |
| A | GLU360 | |
| B | GLY222 | |
| B | ARG245 | |
| B | GLU360 |
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 |
