5DY2

Crystal structure of Dbr2 with mutation M27L

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005737	cellular_component	cytoplasm
A	0005777	cellular_component	peroxisome
A	0005829	cellular_component	cytosol
A	0009695	biological_process	jasmonic acid biosynthetic process
A	0010181	molecular_function	FMN binding
A	0016491	molecular_function	oxidoreductase activity
A	0016628	molecular_function	oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor
A	0016629	molecular_function	12-oxophytodienoate reductase activity
A	0031408	biological_process	oxylipin biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	22
Details	binding site for residue FMN A 401

Chain	Residue
A	ALA25
A	CYS316
A	GLY317
A	GLY318
A	PHE338
A	GLY339
A	ARG340
A	PHE366
A	TYR367
A	HOH603
A	HOH642
A	PRO26
A	HOH656
A	HOH689
A	HOH740
A	LEU27
A	THR28
A	GLY59
A	GLN101
A	HIS180
A	ARG232
A	THR275

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P42593

Chain	Residue	Details
A	LEU186

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:5DXY, ECO:0007744|PDB:5DY3

Chain	Residue	Details
A	LEU27
A	THR60
A	LEU102
A	GLY181
A	ILE233
A	GLY317
A	ARG340
A	THR368

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site_id	SWS_FT_FI3
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|Ref.12, ECO:0007744|PDB:5DXY

Chain	Residue	Details
A	TYR279

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