6VUE
wild-type choline TMA lyase in complex with 1-methyl-1,2,3,6-tetrahydropyridin-3-ol
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016840 | molecular_function | carbon-nitrogen lyase activity |
| A | 0033265 | molecular_function | choline binding |
| A | 0042426 | biological_process | choline catabolic process |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0120525 | molecular_function | choline trimethylamine lyase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016840 | molecular_function | carbon-nitrogen lyase activity |
| B | 0033265 | molecular_function | choline binding |
| B | 0042426 | biological_process | choline catabolic process |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0120525 | molecular_function | choline trimethylamine lyase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue NA A 901 |
| Chain | Residue |
| A | SER746 |
| A | MET748 |
| A | HOH1147 |
| A | HOH1173 |
| A | HOH1235 |
| B | HOH1205 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | binding site for residue RP7 A 902 |
| Chain | Residue |
| A | GLY488 |
| A | CYS489 |
| A | GLU491 |
| A | THR502 |
| A | TYR506 |
| A | LEU698 |
| A | ILE700 |
| A | TYR208 |
| A | ASP216 |
| A | PHE395 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue NA B 901 |
| Chain | Residue |
| A | HOH1194 |
| B | SER746 |
| B | MET748 |
| B | HOH1017 |
| B | HOH1178 |
| B | HOH1200 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue RP7 B 902 |
| Chain | Residue |
| B | TYR208 |
| B | ASP216 |
| B | PHE395 |
| B | GLY488 |
| B | CYS489 |
| B | GLU491 |
| B | TYR506 |
| B | ILE700 |
Functional Information from PROSITE/UniProt
| site_id | PS00850 |
| Number of Residues | 9 |
| Details | GLY_RADICAL_1 Glycine radical domain signature. VvRVAGYSA |
| Chain | Residue | Details |
| A | VAL816-ALA824 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1316 |
| Details | Domain: {"description":"PFL","evidences":[{"source":"PROSITE-ProRule","id":"PRU00887","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 242 |
| Details | Domain: {"description":"Glycine radical","evidences":[{"source":"PROSITE-ProRule","id":"PRU00493","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Cysteine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_02058","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23151509","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24854437","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_02058","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"24854437","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Glycine radical","evidences":[{"source":"HAMAP-Rule","id":"MF_02058","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23151509","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"24854437","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
