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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 0000166 | molecular_function | nucleotide binding |
| 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 | 138 |
| Details | Region: {"description":"SBD1","evidences":[{"source":"UniProtKB","id":"Q42524","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26412334","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BSM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26412334","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BSV","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26412334","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5BSR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"26412334","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
