2C3D
2.15 Angstrom crystal structure of 2-ketopropyl coenzyme M oxidoreductase carboxylase with a coenzyme M disulfide bound at the active site
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 PDB Data
site_id | AC1 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD A1524 |
Chain | Residue |
A | GLY50 |
A | ALA86 |
A | CYS87 |
A | HIS90 |
A | HIS91 |
A | ALA158 |
A | ALA181 |
A | VAL182 |
A | HIS202 |
A | THR225 |
A | GLU314 |
A | GLY52 |
A | GLY352 |
A | ASP353 |
A | MET359 |
A | GLU360 |
A | MET361 |
A | ALA364 |
A | PHE390 |
A | HOH2080 |
A | HOH2082 |
A | HOH2141 |
A | ALA53 |
A | HOH2232 |
A | HOH2323 |
A | HOH2324 |
B | PHE501 |
B | HOH2309 |
A | ALA54 |
A | ASP73 |
A | ARG74 |
A | TRP75 |
A | GLY80 |
A | SER81 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE COM A1525 |
Chain | Residue |
A | ARG56 |
A | PHE57 |
A | GLY79 |
A | MET140 |
A | MET361 |
A | ARG365 |
B | COM1525 |
B | HOH2328 |
site_id | AC3 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE COM A1526 |
Chain | Residue |
A | MET419 |
A | LEU431 |
A | PHE501 |
A | HIS506 |
A | GLN509 |
A | HOH2325 |
A | HOH2326 |
B | MET140 |
B | COM1526 |
site_id | AC4 |
Number of Residues | 34 |
Details | BINDING SITE FOR RESIDUE FAD B1524 |
Chain | Residue |
A | PHE501 |
A | HOH2313 |
B | GLY50 |
B | GLY52 |
B | ALA53 |
B | ALA54 |
B | ASP73 |
B | ARG74 |
B | TRP75 |
B | GLY80 |
B | SER81 |
B | ALA86 |
B | CYS87 |
B | HIS90 |
B | HIS91 |
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 |
B | PHE390 |
B | HOH2038 |
B | HOH2212 |
B | HOH2218 |
B | HOH2325 |
B | HOH2326 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE COM B1525 |
Chain | Residue |
A | MET140 |
A | COM1525 |
B | MET419 |
B | LEU431 |
B | PHE501 |
B | HIS506 |
B | GLN509 |
B | HOH2327 |
B | HOH2328 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE COM B1526 |
Chain | Residue |
B | MET361 |
B | ARG365 |
A | COM1526 |
A | HOH2325 |
B | ARG56 |
B | PHE57 |
B | GLY79 |
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 | PHE501 | |
B | ALA53 | |
B | SER81 | |
B | ALA158 | |
B | ASP353 | |
B | MET361 | |
B | PHE501 | |
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 | 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 |