5BSM
Crystal structure of 4-coumarate:CoA ligase complexed with magnesium and Adenosine triphosphate
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 | 28 |
Details | binding site for residue ATP A 600 |
Chain | Residue |
A | SER189 |
A | PRO311 |
A | GLN331 |
A | GLY332 |
A | TYR333 |
A | GLY334 |
A | MET335 |
A | THR336 |
A | ASP420 |
A | ILE432 |
A | ARG435 |
A | SER190 |
A | LYS526 |
A | MG601 |
A | HOH711 |
A | HOH725 |
A | HOH728 |
A | HOH770 |
A | HOH817 |
A | HOH835 |
A | HOH864 |
A | GLY191 |
A | THR192 |
A | THR193 |
A | LYS197 |
A | HIS237 |
A | ALA309 |
A | ALA310 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue MG A 601 |
Chain | Residue |
A | ATP600 |
A | HOH728 |
A | HOH770 |
A | HOH817 |
A | HOH864 |
site_id | AC3 |
Number of Residues | 26 |
Details | binding site for residue ATP B 600 |
Chain | Residue |
B | SER189 |
B | SER190 |
B | GLY191 |
B | THR192 |
B | THR193 |
B | LYS197 |
B | HIS237 |
B | ALA309 |
B | ALA310 |
B | PRO311 |
B | GLN331 |
B | GLY332 |
B | TYR333 |
B | GLY334 |
B | MET335 |
B | THR336 |
B | ASP420 |
B | ILE432 |
B | ARG435 |
B | LYS526 |
B | MG601 |
B | HOH712 |
B | HOH719 |
B | HOH726 |
B | HOH736 |
B | HOH815 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue MG B 601 |
Chain | Residue |
B | ATP600 |
B | HOH719 |
B | HOH726 |
B | HOH736 |
B | HOH815 |
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 | ASP420 | |
A | ARG435 | |
A | LYS526 | |
B | SER189 | |
B | SER190 | |
B | GLY191 | |
B | THR192 | |
B | THR193 | |
B | LYS197 | |
B | GLN331 | |
A | SER190 | |
B | GLY332 | |
B | THR336 | |
B | ASP420 | |
B | ARG435 | |
B | LYS526 | |
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 | LYS443 | |
B | GLY444 | |
B | GLN446 | |
A | LYS437 | |
A | LYS441 | |
A | LYS443 | |
A | GLY444 | |
A | GLN446 | |
B | LYS260 | |
B | LYS437 | |
B | LYS441 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:26412334 |
Chain | Residue | Details |
A | MET344 | |
B | MET344 |