Structure of PDB 1rrh Chain A

Receptor sequence
>1rrhA (length=850) Species: 3847 (Glycine max) [Search protein sequence]
RGHKIKGTVVLMRKNVLDVNSVTSVGGIIGQGLDLVGSTLDTLTAFLGRS
VSLQLISATKADANGKGKLGKATFLEGIITSLPTLGAGQSAFKINFEWDD
GSGIPGAFYIKNFMQTEFFLVSLTLEDIPNHGSIHFVCNSWIYNAKLFKS
DRIFFANQTYLPSETPAPLVKYREEELHNLRGDGTGERKEWERIYDYDVY
NDLGDPDKGENHARPVLGGNDTFPYPRRGRTGRKPTRKDPNSESRSNDVY
LPRDEAFGHLKSSDFLTYGLKSVSQNVLPLLQSAFDLNFTPREFDSFDEV
HGLYSGGIKLPTDIISKISPLPVLKEIFRTDGEQALKFPPPKVIQVSKSA
WMTDEEFAREMLAGVNPNLIRCLKDFPPRSKLDSQVYGDHTSQITKEHLE
PNLEGLTVDEAIQNKRLFLLDHHDPIMPYLRRINATSTKAYATRTILFLK
NDGTLRPLAIELSLPHPQGDQSGAFSQVFLPADEGVESSIWLLAKAYVVV
NDSCYHQLVSHWLNTHAVVEPFIIATNRHLSVVHPIYKLLHPHYRDTMNI
NGLARLSLVNDGGVIEQTFLWGRYSVEMSAVVYKDWVFTDQALPADLIKR
GMAIEDPSCPHGIRLVIEDYPYTVDGLEIWDAIKTWVHEYVFLYYKSDDT
LREDPELQACWKELVEVGHGDKKNEPWWPKMQTREELVEACAIIIWTASA
LHAAVNFGQYPYGGLILNRPTLSRRFMPEKGSAEYEELRKNPQKAYLKTI
TPKFQTLIDLSVIEILSRHASDEVYLGERDNPNWTSDTRALEAFKRFGNK
LAQIENKLSERNNDEKLRNRCGPVQMPYTLLLPSSKEGLTFRGIPNSISI
3D structure
PDB1rrh Effect of crystal freezing and small-molecule binding on internal cavity size in a large protein: X-ray and docking studies of lipoxygenase at ambient and low temperature at 2.0 A resolution.
ChainA
Resolution2.0 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H518 H523 H709 N713 I857
Catalytic site (residue number reindexed from 1) H511 H516 H702 N706 I850
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 FE2 A H518 H523 H709 I857 H511 H516 H702 I850
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

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:1rrh, PDBe:1rrh, PDBj:1rrh
PDBsum1rrh
PubMed16790932
UniProtP09186|LOX3_SOYBN Seed linoleate 9S-lipoxygenase-3 (Gene Name=LOX1.3)

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