Structure of PDB 4hhs Chain A

Receptor sequence

>4hhsA (length=639) Species: 3702 (Arabidopsis thaliana) [Search protein sequence]

MKVITSLISSILLKFIHKDFHEIYARMSLLDRFLLLIVHGVDKMVPWHKL
PVFLGLTYLEVRRHLHQQYNLLNVGQTPTGIRFDPANYPYRTADGKFNDP
FNEGVGSQNSFFGRNCPPVDQKSKLRRPDPMVVATKLLGRKKFIDTGKQF
NMIAASWIQFMIHDWIDHLEDTHQIELVAPKEVASKCPLSSFRFLKTKEV
PTGFFEIKTGSQNIRTPWWDSSVIYGSNSKTLDRVRTYKDGKLKISEETG
LLLHDEDGLAISGDIRNSWAGVSALQALFIKEHNAVCDALKDEDDDLEDE
DLYRYARLVTSAVVAKIHTIDWTVQLLKTDTLLAGMRANWYGLLGKKFKD
SFGHAGSSILGGVVGMKKPQNHGVPYSLTEDFTSVYRMHSLLPDQLHILD
IDDVPGTNKSLPLIQEISMRDLIGRKGEETMSHIGFTKLMVSMGHQASGA
LELMNYPMWLRDIVPHDPNGQARPDHVDLAALEIYRDRERSVPRYNEFRR
SMFMIPITKWEDLTEDEEAIEVLDDVYDGDVEELDLLVGLMAEKKIKGFA
ISETAFYIFLIMATRRLEADRFFTSDFNETIYTKKGLEWVNTTESLKDVI
DRHYPDMTDKWMNSESAFSVWDSPPLTKNPIPLYLRIPS

3D structure

PDB

4hhs The crystal structure of alpha-Dioxygenase provides insight into diversity in the cyclooxygenase-peroxidase superfamily.

Chain

Resolution

1.7 Å

3D
structure

Catalytic site residues are labeled in the structure
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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.

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)
BS01	HEM	A	I158 Q159 D167 H168 N267 W269 T383 Y386 M388 H389 L392 L479 L482 R486 R490	I158 Q159 D167 H168 N267 W269 T383 Y386 M388 H389 L392 L479 L482 R486 R490
BS02	CA	A	D164 T216 W218 D220 S222	D164 T216 W218 D220 S222
BS03	CA	A	E518 E521	E518 E521
BS04	CA	A	D294 D296	D294 D296
BS05	CL	A	Y386 R566	Y386 R566
BS06	CL	A	K316 N591	K316 N591

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

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component

External links

PDB	RCSB:4hhs, PDBe:4hhs, PDBj:4hhs
PDBsum	4hhs
PubMed	23373518
UniProt	Q9SGH6\|DOX1_ARATH Alpha-dioxygenase 1 (Gene Name=DOX1)

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