2AHV
Crystal Structure of Acyl-CoA transferase from E. coli O157:H7 (YdiF)-thioester complex with CoA- 1
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 | 18 |
| Details | BINDING SITE FOR RESIDUE COA B 2600 |
| Chain | Residue |
| B | ARG288 |
| B | MET397 |
| B | THR399 |
| B | PHE402 |
| B | ILE405 |
| B | GLY421 |
| B | LYS442 |
| B | HOH2697 |
| B | HOH2830 |
| B | HOH2868 |
| B | ASN306 |
| B | VAL309 |
| B | GLY310 |
| B | ILE311 |
| B | SER377 |
| B | ALA379 |
| B | GLU380 |
| B | ASN393 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE COA D 2601 |
| Chain | Residue |
| D | ARG288 |
| D | ASN306 |
| D | VAL309 |
| D | GLY310 |
| D | ILE311 |
| D | GLU333 |
| D | LEU376 |
| D | SER377 |
| D | ALA379 |
| D | GLU380 |
| D | PHE392 |
| D | MET397 |
| D | THR399 |
| D | PHE402 |
| D | ILE405 |
| D | LYS442 |
| D | HOH2691 |
| D | HOH2702 |
| D | HOH2757 |
| D | HOH2952 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE COA A 2602 |
| Chain | Residue |
| A | ARG288 |
| A | ASN306 |
| A | VAL309 |
| A | GLY310 |
| A | ILE311 |
| A | GLU333 |
| A | SER377 |
| A | ALA379 |
| A | GLU380 |
| A | ASN393 |
| A | THR399 |
| A | PHE402 |
| A | ILE405 |
| A | GLY421 |
| A | SER422 |
| A | LYS442 |
| A | HOH2632 |
| A | HOH2722 |
| A | HOH2730 |
| A | HOH2740 |
| A | HOH2776 |
| A | HOH2804 |
| A | HOH2816 |
| site_id | AC4 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE COA C 2603 |
| Chain | Residue |
| C | ARG288 |
| C | VAL309 |
| C | GLY310 |
| C | ILE311 |
| C | GLU333 |
| C | SER377 |
| C | ALA379 |
| C | GLU380 |
| C | PHE392 |
| C | MET397 |
| C | THR399 |
| C | PHE402 |
| C | ILE405 |
| C | ALA420 |
| C | GLY421 |
| C | SER422 |
| C | VAL440 |
| C | HOH2620 |
| C | HOH2671 |
| C | HOH2674 |
| C | HOH2691 |
| C | HOH2712 |
| C | HOH2820 |
| C | HOH2825 |
| C | HOH2881 |
| C | HOH2889 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: 5-glutamyl coenzyme A thioester intermediate => ECO:0000305|PubMed:16253988 |
| Chain | Residue | Details |
| A | GLU333 | |
| B | GLU333 | |
| C | GLU333 | |
| D | GLU333 |
