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6LPV

structure of Spermidine hydroxycinnamoyl transferases from Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0009555biological_processpollen development
A0010584biological_processpollen exine formation
A0016410molecular_functionN-acyltransferase activity
A0016746molecular_functionacyltransferase activity
A0080072molecular_functionspermidine:sinapoyl CoA N-acyltransferase activity
A0080073molecular_functionspermidine:coumaroyl CoA N-acyltransferase activity
A0080074molecular_functionspermidine:caffeoyl CoA N-acyltransferase activity
A0080075molecular_functionspermidine:feruloyl CoA N-acyltransferase activity
A0080088biological_processspermidine hydroxycinnamate conjugate biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues22
Detailsbinding site for residue COA A 501
ChainResidue
AGLY160
ASER326
AASN327
AGLU328
ASER387
ATHR390
ASPD502
AHOH609
AHOH627
AHOH630
AHOH634
AARG246
AHOH647
AHOH652
AHOH677
ATHR262
AARG263
ATYR264
ACYS292
AILE293
AASP294
AARG298

site_idAC2
Number of Residues7
Detailsbinding site for residue SPD A 502
ChainResidue
ATHR33
AHIS155
ACYS292
ATHR312
AASP314
AASP416
ACOA501

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:Q70PR7
ChainResidueDetails
AHIS155
AASP397

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:33519864, ECO:0007744|PDB:6LPV
ChainResidueDetails
ATHR262
AASP294
AARG298
AASP314
ASER387
ATHR33
AHIS155
AGLY160

221051

PDB entries from 2024-06-12

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