2VJQ
Formyl-CoA transferase mutant variant W48Q
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 |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008410 | molecular_function | CoA-transferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0033608 | molecular_function | formyl-CoA transferase activity |
| C | 0033611 | biological_process | oxalate catabolic process |
| D | 0003824 | molecular_function | catalytic activity |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008410 | molecular_function | CoA-transferase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0033608 | molecular_function | formyl-CoA transferase activity |
| D | 0033611 | biological_process | oxalate catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE EPE B 1429 |
| Chain | Residue |
| A | TRP272 |
| B | GLY158 |
| B | ARG238 |
| B | HOH2158 |
| B | HOH2320 |
| B | HOH2321 |
| B | HOH2322 |
| A | GLU273 |
| A | THR274 |
| A | ASP275 |
| A | ALA276 |
| A | HOH2241 |
| A | HOH2245 |
| B | TRP156 |
| B | ASP157 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE EPE D 1429 |
| Chain | Residue |
| C | TRP272 |
| C | GLU273 |
| C | THR274 |
| C | ASP275 |
| C | ALA276 |
| C | HOH2230 |
| C | HOH2236 |
| D | TRP156 |
| D | ASP157 |
| D | GLY158 |
| D | ARG238 |
| D | HOH2267 |
| D | HOH2268 |
| D | HOH2269 |
| D | HOH2270 |
| D | HOH2271 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 52 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| 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 | ASP169 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| C | ASP169 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1xvt |
| Chain | Residue | Details |
| D | ASP169 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 155 |
| Chain | Residue | Details |
| A | GLN17 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU140 | electrostatic stabiliser, hydrogen bond donor |
| A | ASP169 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| A | GLY260 | electrostatic stabiliser, hydrogen bond acceptor |
| A | GLY261 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| 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 | ASP169 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| B | GLY260 | electrostatic stabiliser, hydrogen bond acceptor |
| B | GLY261 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA3 |
| Number of Residues | 5 |
| Details | M-CSA 155 |
| Chain | Residue | Details |
| C | GLN17 | electrostatic stabiliser, hydrogen bond donor |
| C | GLU140 | electrostatic stabiliser, hydrogen bond donor |
| C | ASP169 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| C | GLY260 | electrostatic stabiliser, hydrogen bond acceptor |
| C | GLY261 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA4 |
| Number of Residues | 5 |
| Details | M-CSA 155 |
| Chain | Residue | Details |
| D | GLN17 | electrostatic stabiliser, hydrogen bond donor |
| D | GLU140 | electrostatic stabiliser, hydrogen bond donor |
| D | ASP169 | covalently attached, electrofuge, electrophile, nucleofuge, nucleophile |
| D | GLY260 | electrostatic stabiliser, hydrogen bond acceptor |
| D | GLY261 | electrostatic stabiliser, hydrogen bond donor |
