Structure of PDB 1vji Chain A

Receptor sequence
>1vjiA (length=351) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]
SVPLLTPYKMGRFNLSHRVVLAPLTRQRSYGNVPQPHAAIYYSQRTTPGG
FLITEATGVSDTAQGYQDTPGIWTKEHVEAWKPIVDAVHAKGGIFFCQIW
HVGRVSNSGFQPNGKAPISCSDKPLMPQIRSNGIDEALFTPPRRLGIEEI
PGIVNDFRLAARNAMEAGFDGVEIHGANGYLIDQFMKDTVNDRTDEYGGS
LQNRCKFPLEIVDAVAKEIGPDRVGIRLSPFADYMESGDTNPGALGLYMA
ESLNKYGILYCHVIEARMHTLMPMRKAFKGTFISAGGFTREDGNEAVSKG
RTDLVAYGRWFLANPDLPKRFQVDAPLNKYDRPTFYTSDPVVGYTDYPFL
E
3D structure
PDB1vji X-ray structure of Arabidopsis At1g77680, 12-oxophytodienoate reductase isoform 1.
ChainA
Resolution2.003 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T33 H183 N186 Y188 R235 M243
Catalytic site (residue number reindexed from 1) T25 H175 N178 Y180 R227 M235
Enzyme Commision number 1.3.1.42: 12-oxophytodienoate reductase.
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 FMN A P31 L32 T33 A64 Q106 H183 R235 G304 G305 Y325 G326 R327 F353 Y354 P23 L24 T25 A56 Q98 H175 R227 G286 G287 Y307 G308 R309 F335 Y336
Gene Ontology
Molecular Function
GO:0005515 protein binding
GO:0010181 FMN binding
GO:0016491 oxidoreductase activity
GO:0016629 12-oxophytodienoate reductase activity
Biological Process
GO:0006633 fatty acid biosynthetic process
GO:0031408 oxylipin biosynthetic process
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:1vji, PDBe:1vji, PDBj:1vji
PDBsum1vji
PubMed16080145
UniProtQ8LAH7|OPR1_ARATH 12-oxophytodienoate reductase 1 (Gene Name=OPR1)

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