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1GP4

Anthocyanidin synthase from Arabidopsis thaliana (selenomethionine substituted)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0007033biological_processvacuole organization
A0009611biological_processresponse to wounding
A0009718biological_processanthocyanin-containing compound biosynthetic process
A0009753biological_processresponse to jasmonic acid
A0009813biological_processflavonoid biosynthetic process
A0010023biological_processproanthocyanidin biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0031418molecular_functionL-ascorbic acid binding
A0046148biological_processpigment biosynthetic process
A0046872molecular_functionmetal ion binding
A0050589molecular_functionleucocyanidin oxygenase activity
A0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE AKG A 370
ChainResidue
AASN215
ATYR217
AHIS232
AHIS288
AARG298
ASER300
AALA302
APHE304
AHOH2222

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MES A 376
ChainResidue
ALYS20
AGLU21
AILE23
AARG24
ASER134
AGLN136

Functional Information from PROSITE/UniProt
site_idPS00758
Number of Residues10
DetailsARGE_DAPE_CPG2_1 ArgE / dapE / ACY1 / CPG2 / yscS family signature 1. LGVEAHtDVS
ChainResidueDetails
ALEU227-SER236

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues11
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11796114","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16106293","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qje
ChainResidueDetails
AVAL229

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qje
ChainResidueDetails
ALYS213

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1qje
ChainResidueDetails
AILE122

site_idMCSA1
Number of Residues4
DetailsM-CSA 685
ChainResidueDetails
AVAL229proton acceptor, proton donor, proton relay
AGLY248metal ligand
AGLN250metal ligand
AILE312metal ligand

246031

PDB entries from 2025-12-10

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