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5TMD

Crystal structure of Os79 from O. sativa in complex with U2F and trichothecene.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0008194molecular_functionUDP-glycosyltransferase activity
A0009636biological_processresponse to toxic substance
A0016757molecular_functionglycosyltransferase activity
A0080043molecular_functionquercetin 3-O-glucosyltransferase activity
A0080044molecular_functionquercetin 7-O-glucosyltransferase activity
A0098754biological_processdetoxification
Functional Information from PDB Data
site_idAC1
Number of Residues20
Detailsbinding site for residue U2F A 501
ChainResidue
AGLY26
AGLN346
AHIS361
AGLY363
ATRP364
AASN365
ASER366
AGLU369
AASP385
AGLN386
A7E0502
AHIS27
AHOH800
AASN29
ASER142
AGLN143
ATHR291
AVAL317
APHE343
ACYS344

site_idAC2
Number of Residues4
Detailsbinding site for residue 7E0 A 502
ChainResidue
AHIS27
AMET79
AGLN202
AU2F501

Functional Information from PROSITE/UniProt
site_idPS00375
Number of Residues44
DetailsUDPGT UDP-glycosyltransferases signature. FcpQleVLahkatgCFLSHCGwnStleAIvngv.PLvamPhwaDQ
ChainResidueDetails
APHE343-GLN386

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:A0A0A1HA03
ChainResidueDetails
AHIS27

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Charge relay => ECO:0000250|UniProtKB:A0A0A1HA03
ChainResidueDetails
AASP120

site_idSWS_FT_FI3
Number of Residues12
DetailsBINDING: BINDING => ECO:0000305|PubMed:27715009, ECO:0007744|PDB:5TMD
ChainResidueDetails
AHIS27
ASER142
ATHR291
APHE343
ACYS344
AHIS361
ATRP364
AASN365
ASER366
AGLU369
AASP385
AGLN386

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PDB entries from 2024-05-29

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