2AHW
Crystal Structure of Acyl-CoA transferase from E. coli O157:H7 (YdiF)-thioester complex with CoA- 2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008410 | molecular_function | CoA-transferase activity |
| A | 0008775 | molecular_function | acetate CoA-transferase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046459 | biological_process | short-chain fatty acid metabolic process |
| A | 0046952 | biological_process | ketone body catabolic process |
| A | 0051289 | biological_process | protein homotetramerization |
| B | 0008410 | molecular_function | CoA-transferase activity |
| B | 0008775 | molecular_function | acetate CoA-transferase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0046459 | biological_process | short-chain fatty acid metabolic process |
| B | 0046952 | biological_process | ketone body catabolic process |
| B | 0051289 | biological_process | protein homotetramerization |
| C | 0008410 | molecular_function | CoA-transferase activity |
| C | 0008775 | molecular_function | acetate CoA-transferase activity |
| C | 0016740 | molecular_function | transferase activity |
| C | 0046459 | biological_process | short-chain fatty acid metabolic process |
| C | 0046952 | biological_process | ketone body catabolic process |
| C | 0051289 | biological_process | protein homotetramerization |
| D | 0008410 | molecular_function | CoA-transferase activity |
| D | 0008775 | molecular_function | acetate CoA-transferase activity |
| D | 0016740 | molecular_function | transferase activity |
| D | 0046459 | biological_process | short-chain fatty acid metabolic process |
| D | 0046952 | biological_process | ketone body catabolic process |
| D | 0051289 | biological_process | protein homotetramerization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE COA A 2600 |
| Chain | Residue |
| A | ARG288 |
| A | PHE392 |
| A | MET397 |
| A | THR399 |
| A | PHE402 |
| A | ILE405 |
| A | HOH2631 |
| A | HOH2730 |
| A | HOH2739 |
| A | HOH2767 |
| A | HOH2791 |
| A | VAL309 |
| A | GLY310 |
| A | ILE311 |
| A | GLU333 |
| A | LEU376 |
| A | SER377 |
| A | ALA379 |
| A | GLU380 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE COA B 2600 |
| Chain | Residue |
| B | ARG288 |
| B | ASN306 |
| B | VAL309 |
| B | GLY310 |
| B | ILE311 |
| B | GLU333 |
| B | SER377 |
| B | ALA379 |
| B | GLU380 |
| B | PHE392 |
| B | MET397 |
| B | PHE402 |
| B | ILE405 |
| B | LYS442 |
| B | HOH2677 |
| B | HOH2689 |
| B | HOH2700 |
| B | HOH2750 |
| B | HOH2803 |
| B | HOH2901 |
| site_id | AC3 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE COA C 2600 |
| Chain | Residue |
| C | ARG288 |
| C | ASN306 |
| C | VAL309 |
| C | GLY310 |
| C | ILE311 |
| C | GLU333 |
| C | LEU376 |
| C | SER377 |
| C | ALA379 |
| C | GLU380 |
| C | MET397 |
| C | THR399 |
| C | ILE405 |
| C | ALA420 |
| C | GLY421 |
| C | SER422 |
| C | HOH2617 |
| C | HOH2667 |
| C | HOH2670 |
| C | HOH2685 |
| C | HOH2702 |
| C | HOH2785 |
| C | HOH2788 |
| C | HOH2807 |
| C | HOH2826 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"5-glutamyl coenzyme A thioester intermediate","evidences":[{"source":"PubMed","id":"16253988","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
