Structure of PDB 3dy5 Chain C

Receptor sequence
>3dy5C (length=1002) Species: 47982 (Plexaura homomalla) [Search protein sequence]
WKNFGFEIFGEKYGQEELEKRIKDEHTPPPDSPVFGGLKLKLKKEKFKTL
FTLGTTLKGFRRATHTVGTGGIGEITIVNDPKFPEHEFFTAGRTFPARLR
HANLKYPDDAGADARSFSIKFADSDSDGPLDIVMNTGEANIFWNSPSLED
FVPVEEGDAAEEYVYKNPYYYYNLVEALRRAPDTFAHLYYYSQVTMPFKA
KDGKVRYCRYRALPGDVDIKEEDESGRLTEEEQRKIWIFSRHENEKRPDD
YLRKEYVERLQKGPVNYRLQIQIHEASPDDTATIFHAGILWDKETHPWFD
LAKVSIKTPLSPDVLEKTAFNIANQPASLGLLEAKSPEDYNSIGELRVAV
YTWVQHLRKLKIGSLNAIYNVEVETGDREHAGTDATITIRITGAKGRTDY
LKLFEAGSKEQYTVQGFDVGDIQLIELHSDGGGSGDPDWFVNRVIIISST
QDRVYSFPCFRWVIKDMVLFPGEATLPFNEVPAIVSEQRQKELEQRKLTY
QWDYVSDDMPGNIKAKTHDDLPRDVQFTDEKSRSYQESRKAALVNLGIGS
LWHEDRWFGYQFLNGANPVILTRCDALPSNFPVTNEHVNASLDRGKNLDE
EIKDGHIYIVDFKVLVGAKSYGGPVLEDIGEADIRYCAAPLALFYVNKLG
HLMPIAIQINQEPGPENPIWTPHEENEHDWMMAKFWLGVAESNFHQLNTH
LLRTHLTTESFALSTWRNLASAHPIFKLLQPHIYGVLAIDTIGRKELIGS
GGIVDQSLSLGGGGHVTFMEKCFKEVNLQDYHLPNALKKRGVDDPSKLPG
FYYRDDGLALWEAIETFIGEIIAIFYKNDDDVKRDNEIQSWIYDVHKNGW
RVNPGHQDHGVPASFESREQLKEVLTSLVFTFSCQHAAVNFSQKNAPAIL
RHPPPKKKGEATLQSILSTLPSKSQAAKAIATVYILTKFSEDERYLGNYS
ATAWEDKDALDAINRFQDKLEDISKKIKQRNENLEVPYIYLLPERIPNGT
AI
3D structure
PDB3dy5 A covalent linker allows for membrane targeting of an oxylipin biosynthetic complex.
ChainC
Resolution3.51 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) Y353 H757 H762 H943 I1066
Catalytic site (residue number reindexed from 1) Y351 H700 H705 H886 I1002
Enzyme Commision number 1.13.11.40: arachidonate 8-lipoxygenase.
4.2.1.-
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 FE2 C H757 H762 H943 N947 I1066 H700 H705 H886 N890 I1002
BS02 HEM C R64 T66 H67 R102 S120 M136 N137 F144 Q195 F322 R349 Y353 Q357 R360 R62 T64 H65 R100 S118 M134 N135 F142 Q193 F320 R347 Y351 Q355 R358
Gene Ontology
Molecular Function
GO:0005506 iron ion binding
GO:0009978 allene oxide synthase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0016829 lyase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0047677 arachidonate 8(R)-lipoxygenase activity
GO:0051213 dioxygenase activity
Biological Process
GO:0006631 fatty acid metabolic process
GO:0006633 fatty acid biosynthetic process
GO:0019369 arachidonate metabolic process
GO:0031408 oxylipin biosynthetic process
GO:0034440 lipid oxidation
Cellular Component
GO:0005737 cytoplasm
GO:0016020 membrane

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:3dy5, PDBe:3dy5, PDBj:3dy5
PDBsum3dy5
PubMed18785758
UniProtO16025|AOSL_PLEHO Allene oxide synthase-lipoxygenase protein

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