Structure of PDB 3dsi Chain A Binding Site BS01

Receptor Information
>3dsi Chain A (length=466) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
DLPIRNIPGNYGLPIVGPIKDRWDYFYDQGAEEFFKSRIRKYNSTVYRVN
MPPGAFIAENPQVVALLDGKSFPVLFDVDKVEKKDLFTGTYMPSTELTGG
YRILSYLDPSEPKHEKLKNLLFFLLKSSRNRIFPEFQATYSELFDSLEKE
LSLKGKADFGGSSDGTAFNFLARAFYGTNPADTKLKADAPGLITKWVLFN
LHPLLSIGLPRVIEEPLIHTFSLPPALVKSDYQRLYEFFLESAGEILVEA
DKLGISREEATHNLLFATCFNTWGGMKILFPNMVKRIGRAGHQVHNRLAE
EIRSVIKSNGGELTMGAIEKMELTKSVVYECLRFEPPVTAQYGRAKKDLV
IESHDAAFKVKAGEMLYGYQPLATRDPKIFDRADEFVPERFVGEEGEKLL
RHVLWSNGPETETPTVGNKQCAGKDFVVLVARLFVIEIFRRYDSFDIEVG
TSPLGSSVNFSSLRKA
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain3dsi Chain A Residue 600 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB3dsi Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes
Resolution1.6 Å
Binding residue
(original residue number in PDB)		K133 F137 L154 H164 K168 L171 N321 T322 G325 P387 W455 K469 C471 A472 G473 V477
Binding residue
(residue number reindexed from 1)		K83 F87 L104 H114 K118 L121 N271 T272 G275 P337 W405 K419 C421 A422 G423 V427
Annotation score1
Enzymatic activity
Enzyme Commision number 4.2.1.92: hydroperoxide dehydratase.
Gene Ontology
Molecular Function
GO:0004497 monooxygenase activity
GO:0005506 iron ion binding
GO:0009978 allene oxide synthase activity
GO:0016705 oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
GO:0016829 lyase activity
GO:0019825 oxygen binding
GO:0020037 heme binding
GO:0046872 metal ion binding
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0006952 defense response
GO:0009611 response to wounding
GO:0009620 response to fungus
GO:0009695 jasmonic acid biosynthetic process
GO:0009753 response to jasmonic acid
GO:0019373 epoxygenase P450 pathway
GO:0031407 oxylipin metabolic process
GO:0031408 oxylipin biosynthetic process
GO:0050832 defense response to fungus
Cellular Component
GO:0005739 mitochondrion
GO:0009507 chloroplast
GO:0009534 chloroplast thylakoid
GO:0009535 chloroplast thylakoid membrane
GO:0009536 plastid
GO:0009579 thylakoid
GO:0009941 chloroplast envelope
GO:0010287 plastoglobule

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:3dsi, PDBe:3dsi, PDBj:3dsi
PDBsum3dsi
PubMed18716621
UniProtQ96242|CP74A_ARATH Allene oxide synthase, chloroplastic (Gene Name=CYP74A)

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