2TMD
CORRELATION OF X-RAY DEDUCED AND EXPERIMENTAL AMINO ACID SEQUENCES OF TRIMETHYLAMINE DEHYDROGENASE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| 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 | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| 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 | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 34 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1DJN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TMD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"covalent","evidences":[{"source":"PubMed","id":"1551870","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"620783","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1O94","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O95","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TMD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1DJQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2TMD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"S-6-FMN cysteine"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10224069, 11304539 |
| Chain | Residue | Details |
| A | HIS172 | |
| A | TYR169 | |
| A | ASP267 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | a catalytic site defined by CSA, PubMed 10224069, 11304539 |
| Chain | Residue | Details |
| B | HIS172 | |
| B | TYR169 | |
| B | ASP267 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 114 |
| Chain | Residue | Details |
| A | CYS30 | activator, alter redox potential, covalently attached |
| A | TYR169 | activator, alter redox potential, electrostatic stabiliser, hydrogen bond donor |
| A | HIS172 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | ASP267 | electrostatic stabiliser |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 114 |
| Chain | Residue | Details |
| B | CYS30 | activator, alter redox potential, covalently attached |
| B | TYR169 | activator, alter redox potential, electrostatic stabiliser, hydrogen bond donor |
| B | HIS172 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | ASP267 | electrostatic stabiliser |
