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1CGZ

CHALCONE SYNTHASE FROM ALFALFA COMPLEXED WITH RESVERATROL

Functional Information from GO Data
ChainGOidnamespacecontents
A0009058biological_processbiosynthetic process
A0009715biological_processchalcone biosynthetic process
A0009813biological_processflavonoid biosynthetic process
A0016210molecular_functionnaringenin-chalcone synthase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0030639biological_processpolyketide biosynthetic process
A0102128molecular_functionchalcone synthase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE STL A 390
ChainResidue
AASP255
AGLY256
ATHR264
APHE265
AASN336
ASER338
APRO375
AHOH458
AHOH694
AHOH722
AGLU192
AVAL193
ATHR194
ATHR197
APHE215
AGLY216
AASP217
AILE254

site_idCYS
Number of Residues1
DetailsCATALYTIC SITE
ChainResidue
ACYS164

Functional Information from PROSITE/UniProt
site_idPS00441
Number of Residues17
DetailsCHALCONE_SYNTH Chalcone and stilbene synthases active site. RYmMyQqGCFAGGTvLR
ChainResidueDetails
AARG156-ARG172

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Acyl-thioester intermediate => ECO:0000305
ChainResidueDetails
ACYS164

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS55
AGLY216

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10426957
ChainResidueDetails
ATHR197

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10426957, ECO:0000269|PubMed:10653632
ChainResidueDetails
AALA308

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1cgk
ChainResidueDetails
APHE215
ACYS164
AASN336
AHIS303

site_idMCSA1
Number of Residues4
DetailsM-CSA 355
ChainResidueDetails
ACYS164activator, covalently attached, nucleofuge, nucleophile
APHE215electrostatic destabiliser, polar/non-polar interaction
AHIS303electrostatic stabiliser, hydrogen bond donor
AASN336electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2024-05-01

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