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 | 1 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000269|PubMed:15213226 |
Chain | Residue | Details |
B | A0A169 |
site_id | SWS_FT_FI2 |
Number of Residues | 5 |
Details | BINDING: |
Chain | Residue | Details |
B | ASN96 | |
B | LYS137 | |
B | GLY260 | |
B | HIS15 | |
B | LEU72 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000269|PubMed:12839984, ECO:0000269|PubMed:15213226, ECO:0000269|PubMed:18162462 |
Chain | Residue | Details |
B | ARG38 | |
B | ARG104 |
Catalytic Information from CSA
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 | GLY260 | electrostatic stabiliser, hydrogen bond acceptor |
B | GLY261 | electrostatic stabiliser, hydrogen bond donor |