2TMD
CORRELATION OF X-RAY DEDUCED AND EXPERIMENTAL AMINO ACID SEQUENCES OF TRIMETHYLAMINE DEHYDROGENASE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
A | 0010181 | molecular_function | FMN binding |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0033543 | biological_process | fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway |
A | 0046872 | molecular_function | metal ion binding |
A | 0050470 | molecular_function | trimethylamine dehydrogenase activity |
A | 0051536 | molecular_function | iron-sulfur cluster binding |
A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
B | 0008670 | molecular_function | 2,4-dienoyl-CoA reductase (NADPH) activity |
B | 0010181 | molecular_function | FMN binding |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0033543 | biological_process | fatty acid beta-oxidation, unsaturated, even number, reductase/isomerase pathway |
B | 0046872 | molecular_function | metal ion binding |
B | 0050470 | molecular_function | trimethylamine dehydrogenase activity |
B | 0051536 | molecular_function | iron-sulfur cluster binding |
B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SF4 A 801 |
Chain | Residue |
A | ARG322 |
A | ILE325 |
A | CYS345 |
A | ILE346 |
A | CYS348 |
A | ASN349 |
A | CYS351 |
A | CYS364 |
A | THR365 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE FMN A 802 |
Chain | Residue |
A | VAL27 |
A | PRO28 |
A | HIS29 |
A | CYS30 |
A | GLU59 |
A | TYR60 |
A | GLU103 |
A | TYR169 |
A | HIS172 |
A | ARG222 |
A | TRP264 |
A | ASP267 |
A | VAL297 |
A | ARG299 |
A | CYS320 |
A | ALA321 |
A | ARG322 |
A | PRO323 |
A | HOH811 |
A | HOH865 |
site_id | AC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ADP A 803 |
Chain | Residue |
A | GLY396 |
A | GLY398 |
A | PRO399 |
A | SER400 |
A | ASP419 |
A | THR420 |
A | GLY426 |
A | HIS427 |
A | PRO469 |
A | MET470 |
A | ALA486 |
A | THR487 |
A | GLY488 |
A | GLY673 |
A | ASP674 |
A | HOH804 |
A | HOH848 |
A | HOH911 |
A | HOH1007 |
A | HOH1082 |
site_id | AC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SF4 B 801 |
Chain | Residue |
B | ARG322 |
B | ILE325 |
B | CYS345 |
B | ILE346 |
B | GLY347 |
B | CYS348 |
B | ASN349 |
B | CYS351 |
B | CYS364 |
B | THR365 |
site_id | AC5 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE FMN B 802 |
Chain | Residue |
B | VAL27 |
B | PRO28 |
B | HIS29 |
B | CYS30 |
B | GLU59 |
B | TYR60 |
B | GLU103 |
B | TYR169 |
B | HIS172 |
B | ARG222 |
B | TRP264 |
B | ASP267 |
B | ALA268 |
B | VAL297 |
B | ARG299 |
B | CYS320 |
B | ALA321 |
B | ARG322 |
B | PRO323 |
B | ILE352 |
B | HOH825 |
B | HOH861 |
site_id | AC6 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ADP B 803 |
Chain | Residue |
B | HOH1026 |
B | HOH1045 |
B | GLY396 |
B | GLY398 |
B | PRO399 |
B | SER400 |
B | ASP419 |
B | THR420 |
B | GLY426 |
B | HIS427 |
B | PRO469 |
B | MET470 |
B | ALA486 |
B | THR487 |
B | GLY488 |
B | ASP674 |
B | HOH816 |
B | HOH833 |
B | HOH860 |
B | HOH948 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000250 |
Chain | Residue | Details |
A | LEU175 | |
B | LEU175 |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU104 | |
B | PHE223 | |
B | ALA268 | |
B | PRO323 | |
B | ILE346 | |
B | ASN349 | |
B | ILE352 | |
B | THR365 | |
A | PHE223 | |
A | ALA268 | |
A | PRO323 | |
A | ILE346 | |
A | ASN349 | |
A | ILE352 | |
A | THR365 | |
B | LEU104 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
A | GLY170 | |
A | VAL392 | |
B | GLY170 | |
B | VAL392 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: S-6-FMN cysteine |
Chain | Residue | Details |
A | ILE31 | |
B | ILE31 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 114 |
Chain | Residue | Details |
A | ILE31 | activator, alter redox potential, covalently attached |
A | GLY170 | activator, alter redox potential, electrostatic stabiliser, hydrogen bond donor |
A | SER173 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | ALA268 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 114 |
Chain | Residue | Details |
B | ILE31 | activator, alter redox potential, covalently attached |
B | GLY170 | activator, alter redox potential, electrostatic stabiliser, hydrogen bond donor |
B | SER173 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
B | ALA268 | electrostatic stabiliser |