Structure of PDB 1rov Chain A

Receptor sequence
>1rovA (length=836) Species: 3847 (Glycine max) [Search protein sequence]
GHKIKGTVVLMRKNVLDVNSVTSVTLDTLTAFLGRSVSLQLISATKADAN
GKGKLGKATFLEGIITSLPTLGAGQSAFKINFEWDDGSGIPGAFYIKNFM
QTEFFLVSLTLEDIPNHGSIHFVCNSWIYNAKLFKSDRIFFANQTYLPSE
TPAPLVKYREEELHNLRGDGTGERKEWERIYDYDVYNDLGDPDKGENHAR
PVLGGNDTFPYPRRGRTGRKPTRKDPNSESRSNDVYLPRDEAFGHLKSSD
FLTYGLKSVSQNVLPLLQSAFDLNFTPREFDSFDEVHGLYSGGIKLPTDI
ISKISPLPVLKEIFRTDGEQALKFPPPKVIQVSKSAWMTDEEFAREMLAG
VNPNLIRCLKDFPPRSKLDSQVYGDHTSQITKEHLEPNLEGLTVDEAIQN
KRLFLLDHHDPIMPYLRRINATSTKAYATRTILFLKNDGTLRPLAIELSL
PHPQGDQSGAFSQVFLPADEGVESSIWLLAKAYVVVNDSCYHQLVSHWLN
THAVVEPFIIATNRHLSVVHPIYKLLHPHYRDTMNINGLARLSLVNDGGV
IEQTFLWGRYSVEMSAVVYKDWVFTDQALPADLIKRGMAIEDPSCPHGIR
LVIEDYPYTVDGLEIWDAIKTWVHEYVFLYYKSDDTLREDPELQACWKEL
VEVGHGDKKNEPWWPKMQTREELVEACAIIIWTASALHAAVNFGQYPYGG
LILNRPTLSRRFMPEKGSAEYEELRKNPQKAYLKTITPKFQTLIDLSVIE
ILSRHASDEVYLGERDNPNWTSDTRALEAFKRFGNKLAQIENKLSERNND
EKLRNRCGPVQMPYTLLLPSSKEGLTFRGIPNSISI
3D structure
PDB1rov Interaction between non-heme iron of lipoxygenases and cumene hydroperoxide: basis for enzyme activation, inactivation, and inhibition
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the 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
Catalytic site (original residue number in PDB) H518 H523 H709 N713 I857
Catalytic site (residue number reindexed from 1) H497 H502 H688 N692 I836
Enzyme Commision number 1.13.11.58: linoleate 9S-lipoxygenase.
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 FE A H518 H523 H709 N713 I857 H497 H502 H688 N692 I836
Gene Ontology
Molecular Function
GO:0016491 oxidoreductase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
GO:1990136 linoleate 9S-lipoxygenase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0031408 oxylipin biosynthetic process
GO:0034440 lipid oxidation
Cellular Component
GO:0005737 cytoplasm

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1rov, PDBe:1rov, PDBj:1rov
PDBsum1rov
PubMed14971933
UniProtP09186|LOX3_SOYBN Seed linoleate 9S-lipoxygenase-3 (Gene Name=LOX1.3)

[Back to BioLiP]