8WEV
Crystal structure of Feruoyl-CoA Synthetase complexed with AMP from Amycolatopsis thermoflava
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005524 | molecular_function | ATP binding |
| A | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
| A | 0033494 | biological_process | ferulate metabolic process |
| A | 0042189 | biological_process | vanillin biosynthetic process |
| A | 0050563 | molecular_function | trans-feruloyl-CoA synthase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0016877 | molecular_function | ligase activity, forming carbon-sulfur bonds |
| B | 0033494 | biological_process | ferulate metabolic process |
| B | 0042189 | biological_process | vanillin biosynthetic process |
| B | 0050563 | molecular_function | trans-feruloyl-CoA synthase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. LMYTSGSTGrPK |
| Chain | Residue | Details |
| A | LEU151-LYS162 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q5SKN9","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |






