6LSV

Crystal structure of JOX2 in complex with 2OG, Fe, and JA

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d6lsva_	All beta proteins	Double-stranded beta-helix	Clavaminate synthase-like	automated matches	automated matches	Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)
B	d6lsvb_	All beta proteins	Double-stranded beta-helix	Clavaminate synthase-like	automated matches	automated matches	Mouse-ear cress (Arabidopsis thaliana ) [TaxId: 3702 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	DIOX_N	e6lsvA1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: DIOX_N	ECOD (1.6)
B	DIOX_N	e6lsvB1	A: beta sandwiches	X: jelly-roll	H: Double-stranded beta-helix (From Topology)	T: Double-stranded beta-helix	F: DIOX_N	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF03171	2OG-Fe(II) oxygenase superfamily (2OG-FeII_Oxy)	2OG-Fe(II) oxygenase superfamily	This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily [1]. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reacti ...	This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily [1]. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site [3]. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.	Domain
A, B	PF14226	non-haem dioxygenase in morphine synthesis N-terminal (DIOX_N)	non-haem dioxygenase in morphine synthesis N-terminal	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Probable 2-oxoglutarate-dependent dioxygenase At5g05600	cation binding transition metal ion binding iron ion binding ion binding binding metal ion binding small molecule binding hydrolase activity jasmonic acid hydrolase catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds oxidoreductase activity dioxygenase activity	regulation of defense response regulation of response to biotic stimulus defense response to insect biological process involved in interspecies interaction between organisms response to stimulus negative regulation of response to biotic stimulus regulation of response to external stimulus negative regulation of biological process response to biotic stimulus response to stress regulation of response to stress regulation of defense response to insect response to external biotic stimulus regulation of biological process regulation of defense response regulation of response to biotic stimulus defense response to insect biological process involved in interspecies interaction between organisms response to stimulus negative regulation of response to biotic stimulus regulation of response to external stimulus negative regulation of biological process response to biotic stimulus response to stress regulation of response to stress regulation of defense response to insect response to external biotic stimulus regulation of biological process response to other organism defense response negative regulation of response to stimulus biological regulation response to external stimulus negative regulation of defense response to insect regulation of response to stimulus defense response to other organism negative regulation of response to external stimulus negative regulation of defense response cellular response to stimulus cellular response to chemical stimulus response to chemical cellular process cellular response to toxic substance response to toxic substance regulation of cellular process response to lipid signaling regulation of jasmonic acid mediated signaling pathway regulation of signal transduction hormone-mediated signaling pathway cell communication cellular response to endogenous stimulus cellular response to jasmonic acid stimulus response to hormone signal transduction cellular response to hormone stimulus regulation of signaling response to jasmonic acid response to fatty acid response to endogenous stimulus response to oxygen-containing compound jasmonic acid mediated signaling pathway cellular response to oxygen-containing compound cellular response to fatty acid cellular response to lipid regulation of cell communication defense response to fungus regulation of defense response to fungus response to fungus	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR050295	Plant 2-oxoglutarate-dependent oxidoreductases	Family
A, B	IPR005123	Oxoglutarate/iron-dependent dioxygenase domain	Domain
A, B	IPR027443	Isopenicillin N synthase-like superfamily	Homologous Superfamily
A, B	IPR044861	Isopenicillin N synthase-like, Fe(2+) 2OG dioxygenase domain	Domain
A, B	IPR026992	Non-haem dioxygenase N-terminal domain	Domain

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.