Structure of PDB 4hhs Chain A Binding Site BS02

Receptor Information
>4hhs Chain A (length=639) Species: 3702 (Arabidopsis thaliana) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
MKVITSLISSILLKFIHKDFHEIYARMSLLDRFLLLIVHGVDKMVPWHKL
PVFLGLTYLEVRRHLHQQYNLLNVGQTPTGIRFDPANYPYRTADGKFNDP
FNEGVGSQNSFFGRNCPPVDQKSKLRRPDPMVVATKLLGRKKFIDTGKQF
NMIAASWIQFMIHDWIDHLEDTHQIELVAPKEVASKCPLSSFRFLKTKEV
PTGFFEIKTGSQNIRTPWWDSSVIYGSNSKTLDRVRTYKDGKLKISEETG
LLLHDEDGLAISGDIRNSWAGVSALQALFIKEHNAVCDALKDEDDDLEDE
DLYRYARLVTSAVVAKIHTIDWTVQLLKTDTLLAGMRANWYGLLGKKFKD
SFGHAGSSILGGVVGMKKPQNHGVPYSLTEDFTSVYRMHSLLPDQLHILD
IDDVPGTNKSLPLIQEISMRDLIGRKGEETMSHIGFTKLMVSMGHQASGA
LELMNYPMWLRDIVPHDPNGQARPDHVDLAALEIYRDRERSVPRYNEFRR
SMFMIPITKWEDLTEDEEAIEVLDDVYDGDVEELDLLVGLMAEKKIKGFA
ISETAFYIFLIMATRRLEADRFFTSDFNETIYTKKGLEWVNTTESLKDVI
DRHYPDMTDKWMNSESAFSVWDSPPLTKNPIPLYLRIPS
Ligand information
Ligand IDCA
InChIInChI=1S/Ca/q+2
InChIKeyBHPQYMZQTOCNFJ-UHFFFAOYSA-N
SMILES
SoftwareSMILES
CACTVS 3.341[Ca++]
ACDLabs 10.04
OpenEye OEToolkits 1.5.0		[Ca+2]
FormulaCa
NameCALCIUM ION
ChEMBL
DrugBankDB14577
ZINC
PDB chain4hhs Chain A Residue 702 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
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PDB4hhs The crystal structure of alpha-Dioxygenase provides insight into diversity in the cyclooxygenase-peroxidase superfamily.
Resolution1.7 Å
Binding residue
(original residue number in PDB)		D164 T216 W218 D220 S222
Binding residue
(residue number reindexed from 1)		D164 T216 W218 D220 S222
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) Q159 H163
Catalytic site (residue number reindexed from 1) Q159 H163
Enzyme Commision number 1.13.11.92: fatty acid alpha-dioxygenase.
Gene Ontology
Molecular Function
GO:0004601 peroxidase activity
GO:0016491 oxidoreductase activity
GO:0016702 oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0051213 dioxygenase activity
Biological Process
GO:0001561 fatty acid alpha-oxidation
GO:0006629 lipid metabolic process
GO:0006631 fatty acid metabolic process
GO:0006633 fatty acid biosynthetic process
GO:0006979 response to oxidative stress
GO:0008219 cell death
GO:0009626 plant-type hypersensitive response
GO:0009627 systemic acquired resistance
GO:0009737 response to abscisic acid
GO:0009751 response to salicylic acid
GO:0031408 oxylipin biosynthetic process
GO:0034614 cellular response to reactive oxygen species
GO:0042742 defense response to bacterium
GO:0050832 defense response to fungus
GO:0071446 cellular response to salicylic acid stimulus
GO:0071732 cellular response to nitric oxide
GO:0098869 cellular oxidant detoxification
GO:1902609 (R)-2-hydroxy-alpha-linolenic acid biosynthetic process
Cellular Component
GO:0005811 lipid droplet
GO:0012511 monolayer-surrounded lipid storage body

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Molecular Function
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Biological Process
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Cellular Component
External links
PDB RCSB:4hhs, PDBe:4hhs, PDBj:4hhs
PDBsum4hhs
PubMed23373518
UniProtQ9SGH6|DOX1_ARATH Alpha-dioxygenase 1 (Gene Name=DOX1)

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