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2QX7

Structure of Eugenol Synthase from Ocimum basilicum

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0009698biological_processphenylpropanoid metabolic process
A0009699biological_processphenylpropanoid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0042803molecular_functionprotein homodimerization activity
A0042855biological_processeugenol biosynthetic process
B0000166molecular_functionnucleotide binding
B0009698biological_processphenylpropanoid metabolic process
B0009699biological_processphenylpropanoid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0042803molecular_functionprotein homodimerization activity
B0042855biological_processeugenol biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAP A 401
ChainResidue
ATHR16
AALA84
APHE85
AGLN87
ASER110
AASP111
APHE112
AGLY113
ALYS132
AASN152
APHE154
AGLY17
APHE158
AHOH1002
AHOH1016
AHOH1023
AHOH1025
AHOH1030
AHOH1052
AHOH1086
AHOH1108
AHOH1117
ATYR18
AHOH1215
AHOH1336
AILE19
ATHR38
AARG39
ALYS44
AALA82
ALEU83

site_idAC2
Number of Residues31
DetailsBINDING SITE FOR RESIDUE NAP B 401
ChainResidue
BTHR16
BGLY17
BTYR18
BILE19
BTHR38
BARG39
BLYS44
BALA82
BLEU83
BALA84
BPHE85
BGLN87
BSER110
BASP111
BPHE112
BGLY113
BLYS132
BASN152
BCYS153
BPHE154
BPHE158
BHOH1006
BHOH1007
BHOH1015
BHOH1039
BHOH1040
BHOH1049
BHOH1057
BHOH1060
BHOH1083
BHOH1209

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor/acceptor => ECO:0000269|PubMed:17912370
ChainResidueDetails
ALYS132
BLYS132

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:17912370, ECO:0000269|PubMed:18208524, ECO:0007744|PDB:2QW8, ECO:0007744|PDB:2QX7, ECO:0007744|PDB:2QZZ, ECO:0007744|PDB:2R2G, ECO:0007744|PDB:2R6J, ECO:0007744|PDB:3C3X
ChainResidueDetails
ATHR16
ATHR38
ASER110
AASN152
BTHR16
BTHR38
BSER110
BASN152

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:D0VWT0
ChainResidueDetails
AARG39
BARG39

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17912370, ECO:0007744|PDB:2QW8, ECO:0007744|PDB:2QX7, ECO:0007744|PDB:2QZZ, ECO:0007744|PDB:2R2G, ECO:0007744|PDB:2R6J
ChainResidueDetails
APHE85
BPHE85

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:17912370, ECO:0007744|PDB:2QZZ, ECO:0007744|PDB:2R2G
ChainResidueDetails
AVAL114
BVAL114

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:17912370, ECO:0007744|PDB:2QW8, ECO:0007744|PDB:2QX7, ECO:0007744|PDB:2QZZ, ECO:0007744|PDB:2R6J
ChainResidueDetails
ALYS132
BLYS132

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:17912370, ECO:0007744|PDB:2QZZ
ChainResidueDetails
APRO258
BPRO258

site_idSWS_FT_FI8
Number of Residues4
DetailsSITE: Confers substrate specificity => ECO:0000269|PubMed:18208524
ChainResidueDetails
APHE85
AILE88
BPHE85
BILE88

site_idSWS_FT_FI9
Number of Residues2
DetailsSITE: Required for activity => ECO:0000269|PubMed:17912370
ChainResidueDetails
AILE261
BILE261

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PDB entries from 2024-07-10

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