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6D3I

ftv7 dioxygenase with 2,4-D bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0009056biological_processcatabolic process
A0016491molecular_functionoxidoreductase activity
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
D0005737cellular_componentcytoplasm
D0009056biological_processcatabolic process
D0016491molecular_functionoxidoreductase activity
D0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
D0046872molecular_functionmetal ion binding
D0051213molecular_functiondioxygenase activity
G0005737cellular_componentcytoplasm
G0009056biological_processcatabolic process
G0016491molecular_functionoxidoreductase activity
G0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
G0046872molecular_functionmetal ion binding
G0051213molecular_functiondioxygenase activity
J0005737cellular_componentcytoplasm
J0009056biological_processcatabolic process
J0016491molecular_functionoxidoreductase activity
J0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
J0046872molecular_functionmetal ion binding
J0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CO A 301
ChainResidue
AHIS111
AASP113
AHIS270
AAKG302

site_idAC2
Number of Residues10
Detailsbinding site for residue AKG A 302
ChainResidue
ATHR138
AALA272
AARG281
AARG285
ACO301
AILE95
AILE106
AGLY107
AHIS111
AASP113

site_idAC3
Number of Residues4
Detailsbinding site for residue CO G 301
ChainResidue
GHIS111
GASP113
GHIS270
GAKG302

site_idAC4
Number of Residues9
Detailsbinding site for residue AKG G 302
ChainResidue
GILE95
GHIS111
GASP113
GTHR138
GHIS270
GALA272
GARG281
GARG285
GCO301

site_idAC5
Number of Residues10
Detailsbinding site for residue CFA G 303
ChainResidue
GLEU83
GARG104
GILE106
GHIS111
GASP113
GSER114
GVAL170
GPHE182
GVAL220
GTYR221

site_idAC6
Number of Residues4
Detailsbinding site for residue CO D 301
ChainResidue
DHIS111
DASP113
DHIS270
DAKG302

site_idAC7
Number of Residues9
Detailsbinding site for residue AKG D 302
ChainResidue
DILE95
DHIS111
DASP113
DTHR138
DHIS270
DALA272
DARG281
DARG285
DCO301

site_idAC8
Number of Residues8
Detailsbinding site for residue CFA D 303
ChainResidue
DVAL80
DILE82
DILE106
DGLY107
DHIS111
DASP113
DSER114
DTYR221

site_idAC9
Number of Residues4
Detailsbinding site for residue CO J 301
ChainResidue
JHIS111
JASP113
JHIS270
JAKG302

site_idAD1
Number of Residues10
Detailsbinding site for residue AKG J 302
ChainResidue
JGLY107
JHIS111
JASP113
JTHR138
JTRP263
JHIS270
JALA272
JARG281
JARG285
JCO301

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P37610
ChainResidueDetails
AHIS111
GTRP255
GHIS270
GARG281
DHIS111
DASP113
DTHR138
DTRP255
DHIS270
DARG281
JHIS111
AASP113
JASP113
JTHR138
JTRP255
JHIS270
JARG281
ATHR138
ATRP255
AHIS270
AARG281
GHIS111
GASP113
GTHR138

site_idSWS_FT_FI2
Number of Residues8
DetailsSITE: Contributes to enantiospecificity => ECO:0000303|PubMed:16731970
ChainResidueDetails
ATYR221
AARG285
GTYR221
GARG285
DTYR221
DARG285
JTYR221
JARG285

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PDB entries from 2024-08-28

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