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3HBJ

Structure of UGT78G1 complexed with UDP

Functional Information from GO Data
ChainGOidnamespacecontents
A0008194molecular_functionUDP-glycosyltransferase activity
A0009698biological_processphenylpropanoid metabolic process
A0009813biological_processflavonoid biosynthetic process
A0016757molecular_functionglycosyltransferase activity
Functional Information from PDB Data
site_idAC1
Number of Residues18
DetailsBINDING SITE FOR RESIDUE UDP A 900
ChainResidue
ATHR25
AHIS352
AGLY354
ATRP355
AASN356
ASER357
AGLU360
AHOH542
AHOH548
AHOH627
ALYS256
ATYR277
ASER279
ASER282
ASER308
ATRP334
AALA335
AGLN337

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:A0A0A1HA03
ChainResidueDetails
AHIS26

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Charge relay => ECO:0000250|UniProtKB:A0A0A1HA03
ChainResidueDetails
AASP124

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:19683002, ECO:0007744|PDB:3HBF, ECO:0007744|PDB:3HBJ
ChainResidueDetails
ATHR25
ASER282
ASER308
ATRP334

site_idSWS_FT_FI4
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:19683002, ECO:0007744|PDB:3HBF
ChainResidueDetails
AARG89
AHIS155
AGLU192
APHE202
AGLY375

site_idSWS_FT_FI5
Number of Residues9
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:A0A0A1HA03
ChainResidueDetails
AALA335
AGLN337
AHIS352
ATRP355
AASN356
ASER357
AGLU360
AASP376
AGLN377

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PDB entries from 2024-08-21

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