2VJM
Formyl-CoA transferase with aspartyl-formyl anhydide intermediate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008410 | molecular_function | CoA-transferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0033608 | molecular_function | formyl-CoA transferase activity |
| A | 0033611 | biological_process | oxalate catabolic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0008410 | molecular_function | CoA-transferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0033608 | molecular_function | formyl-CoA transferase activity |
| B | 0033611 | biological_process | oxalate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE COA A1169 |
| Chain | Residue |
| A | HIS15 |
| A | ARG104 |
| A | MET105 |
| A | VAL124 |
| A | LYS137 |
| A | VAL138 |
| A | ASP169 |
| A | MET200 |
| A | HOH2170 |
| A | HOH2171 |
| A | HOH2172 |
| A | ALA18 |
| A | HOH2174 |
| A | ARG38 |
| A | LEU72 |
| A | MET74 |
| A | LYS75 |
| A | ASN96 |
| A | PHE97 |
| A | GLY98 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A1429 |
| Chain | Residue |
| A | ASP294 |
| A | ASP297 |
| A | HOH2287 |
| A | HOH2418 |
| A | HOH2419 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE COA B1429 |
| Chain | Residue |
| A | LYS52 |
| B | HIS15 |
| B | VAL16 |
| B | GLN17 |
| B | ALA18 |
| B | ARG38 |
| B | LEU72 |
| B | MET74 |
| B | LYS75 |
| B | ASN96 |
| B | PHE97 |
| B | GLY98 |
| B | ALA101 |
| B | ARG104 |
| B | MET105 |
| B | LYS137 |
| B | VAL138 |
| B | A0A169 |
| B | MET200 |
| B | HOH2138 |
| B | HOH2315 |
| B | HOH2316 |
| B | HOH2317 |
| B | HOH2318 |
| B | HOH2319 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE EPE B1430 |
| Chain | Residue |
| A | TRP272 |
| A | GLU273 |
| A | THR274 |
| A | ASP275 |
| A | ALA276 |
| A | HOH2271 |
| B | TRP156 |
| B | ASP157 |
| B | GLY158 |
| B | ARG238 |
| B | HOH2158 |
| B | HOH2320 |
| B | HOH2321 |
| B | HOH2322 |
| B | HOH2323 |
| B | HOH2324 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15213226","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00742","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12839984","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15213226","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18162462","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| A | ASP169 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| B | A0A169 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 155 |
| Chain | Residue | Details |
| B | GLN17 | electrostatic stabiliser, hydrogen bond donor |
| B | GLU140 | electrostatic stabiliser, hydrogen bond donor |
| B | A0A169 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| B | GLY264 | electrostatic stabiliser, hydrogen bond acceptor |
| B | TRP265 | electrostatic stabiliser, hydrogen bond donor |
