Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6IJA

Crystal Structure of Arabidopsis thaliana UGT89C1 complexed with UDP-L-rhamnose

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0005829cellular_componentcytosol
A0008194molecular_functionUDP-glycosyltransferase activity
A0016757molecular_functionglycosyltransferase activity
A0051555biological_processflavonol biosynthetic process
A0103077molecular_functionquercetin 3-glucoside 7-O-rhamnosyltransferase activity
A0103078molecular_functionquercetin 3-rhamnoside 7-O-rhamnosyltransferase activity
B0005576cellular_componentextracellular region
B0005829cellular_componentcytosol
B0008194molecular_functionUDP-glycosyltransferase activity
B0016757molecular_functionglycosyltransferase activity
B0051555biological_processflavonol biosynthetic process
B0103077molecular_functionquercetin 3-glucoside 7-O-rhamnosyltransferase activity
B0103078molecular_functionquercetin 3-rhamnoside 7-O-rhamnosyltransferase activity
C0005576cellular_componentextracellular region
C0005829cellular_componentcytosol
C0008194molecular_functionUDP-glycosyltransferase activity
C0016757molecular_functionglycosyltransferase activity
C0051555biological_processflavonol biosynthetic process
C0103077molecular_functionquercetin 3-glucoside 7-O-rhamnosyltransferase activity
C0103078molecular_functionquercetin 3-rhamnoside 7-O-rhamnosyltransferase activity
D0005576cellular_componentextracellular region
D0005829cellular_componentcytosol
D0008194molecular_functionUDP-glycosyltransferase activity
D0016757molecular_functionglycosyltransferase activity
D0051555biological_processflavonol biosynthetic process
D0103077molecular_functionquercetin 3-glucoside 7-O-rhamnosyltransferase activity
D0103078molecular_functionquercetin 3-rhamnoside 7-O-rhamnosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
Detailsbinding site for residue AWU A 900
ChainResidue
AGLN18
AGLN317
AHIS332
AGLY334
ATRP335
AGLY336
ASER337
AGLU340
AALA355
AASP356
AGLY20
AHIS21
ALEU88
AILE148
AGLY249
ASER250
ATRP314
AALA315

site_idAC2
Number of Residues16
Detailsbinding site for residue AWU B 900
ChainResidue
BGLN18
BGLY20
BPRO147
BILE148
BGLY249
BTRP314
BALA315
BGLN317
BHIS332
BTRP335
BGLY336
BSER337
BGLU340
BALA355
BASP356
BHIS357

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:A0A0A1HA03
ChainResidueDetails
AHIS21
BHIS21
CHIS21
DHIS21

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Charge relay => ECO:0000250|UniProtKB:A0A0A1HA03
ChainResidueDetails
AASP119
BASP119
CASP119
DASP119

site_idSWS_FT_FI3
Number of Residues28
DetailsBINDING: BINDING => ECO:0000269|PubMed:30893500, ECO:0007744|PDB:6IJA
ChainResidueDetails
AGLN18
ASER250
AALA315
AHIS332
AGLY336
ASER337
AGLU340
BGLN18
BSER250
BALA315
BHIS332
BGLY336
BSER337
BGLU340
CGLN18
CSER250
CALA315
CHIS332
CGLY336
CSER337
CGLU340
DGLN18
DSER250
DALA315
DHIS332
DGLY336
DSER337
DGLU340

site_idSWS_FT_FI4
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:30893500, ECO:0007744|PDB:6IJD
ChainResidueDetails
AHIS21
BHIS21
CHIS21
DHIS21

221051

PDB entries from 2024-06-12

PDB statisticsPDBj update infoContact PDBjnumon