5BSW
Crystal structure of 4-coumarate:CoA ligase delta-V341 mutant complexed with feruloyl adenylate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0009611 | biological_process | response to wounding |
| A | 0009698 | biological_process | phenylpropanoid metabolic process |
| A | 0009753 | biological_process | response to jasmonic acid |
| A | 0016207 | molecular_function | 4-coumarate-CoA ligase activity |
| A | 0016405 | molecular_function | CoA-ligase activity |
| A | 0016874 | molecular_function | ligase activity |
| A | 0050563 | molecular_function | trans-feruloyl-CoA synthase activity |
| A | 0106286 | molecular_function | (E)-caffeate-CoA ligase activity |
| A | 0106290 | molecular_function | trans-cinnamate-CoA ligase activity |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0009611 | biological_process | response to wounding |
| B | 0009698 | biological_process | phenylpropanoid metabolic process |
| B | 0009753 | biological_process | response to jasmonic acid |
| B | 0016207 | molecular_function | 4-coumarate-CoA ligase activity |
| B | 0016405 | molecular_function | CoA-ligase activity |
| B | 0016874 | molecular_function | ligase activity |
| B | 0050563 | molecular_function | trans-feruloyl-CoA synthase activity |
| B | 0106286 | molecular_function | (E)-caffeate-CoA ligase activity |
| B | 0106290 | molecular_function | trans-cinnamate-CoA ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | binding site for residue 4UW A 600 |
| Chain | Residue |
| A | SER189 |
| A | GLY332 |
| A | TYR333 |
| A | GLY334 |
| A | MET335 |
| A | THR336 |
| A | PRO340 |
| A | MET343 |
| A | ASP419 |
| A | ARG434 |
| A | LYS525 |
| A | HIS237 |
| A | HOH744 |
| A | HOH855 |
| A | ILE238 |
| A | TYR239 |
| A | SER243 |
| A | ALA309 |
| A | ALA310 |
| A | PRO311 |
| A | GLN331 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | binding site for residue 4UW B 600 |
| Chain | Residue |
| B | SER189 |
| B | HIS237 |
| B | ILE238 |
| B | TYR239 |
| B | SER243 |
| B | ALA309 |
| B | ALA310 |
| B | PRO311 |
| B | GLN331 |
| B | GLY332 |
| B | TYR333 |
| B | GLY334 |
| B | MET335 |
| B | THR336 |
| B | PRO340 |
| B | MET343 |
| B | ASP419 |
| B | ARG434 |
| B | LYS525 |
| B | HOH736 |
| B | HOH741 |
| B | HOH754 |
| B | HOH848 |
Functional Information from PROSITE/UniProt
| site_id | PS00455 |
| Number of Residues | 12 |
| Details | AMP_BINDING Putative AMP-binding domain signature. LPYSSGTTGlPK |
| Chain | Residue | Details |
| A | LEU186-LYS197 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 24 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26412334, ECO:0007744|PDB:5BSM |
| Chain | Residue | Details |
| A | SER189 | |
| A | ILE420 | |
| A | LEU435 | |
| A | ILE526 | |
| B | SER189 | |
| B | SER190 | |
| B | GLY191 | |
| B | THR192 | |
| B | THR193 | |
| B | LYS197 | |
| B | GLN331 | |
| A | SER190 | |
| B | GLY332 | |
| B | THR336 | |
| B | ILE420 | |
| B | LEU435 | |
| B | ILE526 | |
| A | GLY191 | |
| A | THR192 | |
| A | THR193 | |
| A | LYS197 | |
| A | GLN331 | |
| A | GLY332 | |
| A | THR336 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26412334, ECO:0007744|PDB:5BSV |
| Chain | Residue | Details |
| A | TYR239 | |
| A | SER243 | |
| A | ALA309 | |
| B | TYR239 | |
| B | SER243 | |
| B | ALA309 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26412334, ECO:0007744|PDB:5BSR |
| Chain | Residue | Details |
| A | LYS260 | |
| B | GLY443 | |
| B | PHE444 | |
| B | VAL446 | |
| A | GLU437 | |
| A | TYR441 | |
| A | GLY443 | |
| A | PHE444 | |
| A | VAL446 | |
| B | LYS260 | |
| B | GLU437 | |
| B | TYR441 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26412334 |
| Chain | Residue | Details |
| A | CYS344 | |
| B | CYS344 |
