2VJL
Formyl-CoA transferase with aspartyl-CoA thioester intermediate derived from formyl-CoA
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 | 19 |
Details | BINDING SITE FOR RESIDUE COA A1169 |
Chain | Residue |
A | HIS15 |
A | MET105 |
A | VAL124 |
A | LYS137 |
A | VAL138 |
A | TYR139 |
A | ASP169 |
A | MET200 |
A | HOH2115 |
A | HOH2137 |
A | HOH2138 |
A | ALA18 |
A | ARG38 |
A | LEU72 |
A | MET74 |
A | ASN96 |
A | PHE97 |
A | GLY98 |
A | ARG104 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A3000 |
Chain | Residue |
A | GLN17 |
A | PHE63 |
A | ALA166 |
A | ASP169 |
A | SER170 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A4000 |
Chain | Residue |
A | ASP294 |
A | ASP297 |
A | HOH2245 |
A | HOH2294 |
A | HOH2363 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A4001 |
Chain | Residue |
A | GLY222 |
A | PHE245 |
A | ILE248 |
A | HOH2161 |
A | HOH2168 |
A | HOH2198 |
site_id | AC5 |
Number of Residues | 26 |
Details | BINDING SITE FOR RESIDUE COA B1169 |
Chain | Residue |
A | LYS52 |
A | GLY260 |
A | HOH2219 |
B | HIS15 |
B | VAL16 |
B | GLN17 |
B | ARG38 |
B | LEU72 |
B | ASP73 |
B | MET74 |
B | LYS75 |
B | PHE97 |
B | GLY98 |
B | ARG104 |
B | MET105 |
B | TYR139 |
B | GLU140 |
B | ASP169 |
B | HOH2016 |
B | HOH2160 |
B | HOH2161 |
B | HOH2162 |
B | HOH2163 |
B | HOH2164 |
B | HOH2165 |
B | CL3001 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B3000 |
Chain | Residue |
B | GLN17 |
B | ALA18 |
B | ASP169 |
B | HOH2096 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B3001 |
Chain | Residue |
A | GLY261 |
A | GLN262 |
A | HOH2024 |
B | TYR139 |
B | COA1169 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000269|PubMed:15213226 |
Chain | Residue | Details |
A | ASP169 | |
B | ASP169 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS15 | |
B | GLY260 | |
A | LEU72 | |
A | ASN96 | |
A | LYS137 | |
A | GLY260 | |
B | HIS15 | |
B | LEU72 | |
B | ASN96 | |
B | LYS137 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00742, ECO:0000269|PubMed:12839984, ECO:0000269|PubMed:15213226, ECO:0000269|PubMed:18162462 |
Chain | Residue | Details |
A | ARG38 | |
A | ARG104 | |
B | ARG38 | |
B | ARG104 |
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 | 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 |