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1D6H

CHALONE SYNTHASE (N336A MUTANT COMPLEXED WITH COA)

Functional Information from GO Data
ChainGOidnamespacecontents
A0009058biological_processbiosynthetic process
A0009715biological_processchalcone biosynthetic process
A0009813biological_processflavonoid biosynthetic process
A0016210molecular_functionnaringenin-chalcone synthase activity
A0016740molecular_functiontransferase activity
A0016746molecular_functionacyltransferase activity
A0016747molecular_functionacyltransferase activity, transferring groups other than amino-acyl groups
A0030639biological_processpolyketide biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 391
ChainResidue
ASER3
AVAL4
ASER5
AARG385

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE COA A 390
ChainResidue
ALEU267
AVAL271
APRO272
AGLY305
AGLY306
APRO307
AALA308
AHOH567
ALYS55
AARG58
AMET59
ALYS62
ALEU206

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
ACSD164

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_idMCSA1
Number of Residues4
DetailsM-CSA 355
ChainResidueDetails
APHE165activator, covalently attached, nucleofuge, nucleophile
AALA219electrostatic destabiliser, polar/non-polar interaction
APRO307electrostatic stabiliser, hydrogen bond donor
AALA340electrostatic stabiliser, hydrogen bond donor

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PDB entries from 2025-06-18

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