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5BSV

Crystal structure of 4-coumarate:CoA ligase complexed with feruloyl adenylate

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0009611biological_processresponse to wounding
A0009698biological_processphenylpropanoid metabolic process
A0009753biological_processresponse to jasmonic acid
A0016207molecular_function4-coumarate-CoA ligase activity
A0016405molecular_functionCoA-ligase activity
A0016874molecular_functionligase activity
A0050563molecular_functiontrans-feruloyl-CoA synthase activity
A0106286molecular_function(E)-caffeate-CoA ligase activity
A0106290molecular_functiontrans-cinnamate-CoA ligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue 4UW A 600
ChainResidue
AHIS237
AGLY334
AMET335
ATHR336
AVAL341
AMET344
AASP420
AARG435
ALYS437
ALYS441
AGLN446
ATYR239
AHOH757
AHOH816
AHOH898
ASER243
AALA309
AALA310
APRO311
AGLN331
AGLY332
ATYR333

Functional Information from PROSITE/UniProt
site_idPS00455
Number of Residues12
DetailsAMP_BINDING Putative AMP-binding domain signature. LPYSSGTTGlPK
ChainResidueDetails
ALEU186-LYS197

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:26412334, ECO:0007744|PDB:5BSM
ChainResidueDetails
ASER189
AASP420
AARG435
ALYS526
ASER190
AGLY191
ATHR192
ATHR193
ALYS197
AGLN331
AGLY332
ATHR336

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:26412334, ECO:0007744|PDB:5BSV
ChainResidueDetails
ATYR239
ASER243
AALA309

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:26412334, ECO:0007744|PDB:5BSR
ChainResidueDetails
ALYS260
ALYS437
ALYS441
ALYS443
AGLY444
AGLN446

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:26412334
ChainResidueDetails
AMET344

223166

PDB entries from 2024-07-31

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