Home Research COVID-19 Services Publications People Teaching Job Opening News Forum Lab Only
Online Services

●I-TASSER ●I-TASSER-MTD ●C-I-TASSER ●CR-I-TASSER ●QUARK ●C-QUARK ●LOMETS ●MUSTER ●CEthreader ●SEGMER ●DeepFold ●DeepFoldRNA ●FoldDesign ●COFACTOR ●COACH ●MetaGO ●TripletGO ●IonCom ●FG-MD ●ModRefiner ●REMO ●DEMO ●DEMO-EM ●SPRING ●COTH ●Threpp ●PEPPI ●BSpred ●ANGLOR ●EDock ●BSP-SLIM ●SAXSTER ●FUpred ●ThreaDom ●ThreaDomEx ●EvoDesign ●BindProf ●BindProfX ●SSIPe ●GPCR-I-TASSER ●MAGELLAN ●ResQ ●STRUM ●DAMpred

●TM-score ●TM-align ●US-align ●MM-align ●RNA-align ●NW-align ●LS-align ●EDTSurf ●MVP ●MVP-Fit ●SPICKER ●HAAD ●PSSpred ●3DRobot ●MR-REX ●I-TASSER-MR ●SVMSEQ ●NeBcon ●ResPRE ●TripletRes ●DeepPotential ●WDL-RF ●ATPbind ●DockRMSD ●DeepMSA ●FASPR ●EM-Refiner ●GPU-I-TASSER

●BioLiP ●E. coli ●GLASS ●GPCR-HGmod ●GPCR-RD ●GPCR-EXP ●Tara-3D ●TM-fold ●DECOYS ●POTENTIAL ●RW/RWplus ●EvoEF ●HPSF ●THE-DB ●ADDRESS ●Alpaca-Antibody ●CASP7 ●CASP8 ●CASP9 ●CASP10 ●CASP11 ●CASP12 ●CASP13 ●CASP14

BioLiP

Structure of PDB 3dsk Chain A

Receptor sequence
>3dskA (length=466) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
DLPIRNIPGNYGLPIVGPIKDRWDYFYDQGAEEFFKSRIRKYNSTVYRVN
MPPGAFIAENPQVVALLDGKSFPVLFDVDKVEKKDLLTGTYMPSTELTGG
YRILSYLDPSEPKHEKLKNLLFFLLKSSRNRIFPEFQATYSELFDSLEKE
LSLKGKADFGGSSDGTAFNFLARAFYGTNPADTKLKADAPGLITKWVLFN
LHPLLSIGLPRVIEEPLIHTFSLPPALVKSDYQRLYEFFLESAGEILVEA
DKLGISREEATHNLLFATCFNTWGGMKILFPNMVKRIGRAGHQVHNRLAE
EIRSVIKSNGGELTMGAIEKMELTKSVVYECLRFEPPVTAQYGRAKKDLV
IESHDAAFKVKAGEMLYGYQPLATRDPKIFDRADEFVPERFVGEEGEKLL
RHVLWSNGPETETPTVGNKQCAGKDFVVLVARLFVIEIFRRYDSFDIEVG
TSPLGSSVNFSSLRKA
3D structure
PDB3dsk Structural insights into the evolutionary paths of oxylipin biosynthetic enzymes
ChainA
Resolution1.55 Å
3D
structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Enzyme Commision number 4.2.1.92: hydroperoxide dehydratase.
Interaction with ligand
Site
#		 Ligand Ligand
chain		 Binding residues on receptor
(original residue number in PDB)		 Binding residues on receptor
(residue number reindexed from 1)		 Binding affinity
BS01 HEM A K133 L137 L154 S155 H164 K168 L171 N321 T322 G325 P387 W455 K469 C471 A472 G473 V477 K83 L87 L104 S105 H114 K118 L121 N271 T272 G275 P337 W405 K419 C421 A422 G423 V427
BS02 T25 A L137 F320 N321 G324 V388 T389 A390 L87 F270 N271 G274 V338 T339 A340
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:3dsk, PDBe:3dsk, PDBj:3dsk
PDBsum3dsk
PubMed18716621
UniProtQ96242|CP74A_ARATH Allene oxide synthase, chloroplastic (Gene Name=CYP74A)

[Back to BioLiP]

zhanglabzhanggroup.org | +65-6601-1241 | Computing 1, 13 Computing Drive, Singapore 117417