2RCM

Crystal Structure of Arabidopsis thaliana Allene Oxide Synthase variant (F137L) (At-AOS(F137L), cytochrome P450 74A) at 1.73 A Resolution

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004497	molecular_function	monooxygenase activity
A	0005506	molecular_function	iron ion binding
A	0005739	cellular_component	mitochondrion
A	0006629	biological_process	lipid metabolic process
A	0006631	biological_process	fatty acid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006952	biological_process	defense response
A	0009507	cellular_component	chloroplast
A	0009534	cellular_component	chloroplast thylakoid
A	0009535	cellular_component	chloroplast thylakoid membrane
A	0009536	cellular_component	plastid
A	0009579	cellular_component	thylakoid
A	0009611	biological_process	response to wounding
A	0009620	biological_process	response to fungus
A	0009695	biological_process	jasmonic acid biosynthetic process
A	0009753	biological_process	response to jasmonic acid
A	0009941	cellular_component	chloroplast envelope
A	0009978	molecular_function	allene oxide synthase activity
A	0010287	cellular_component	plastoglobule
A	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
A	0016829	molecular_function	lyase activity
A	0016836	molecular_function	hydro-lyase activity
A	0019373	biological_process	epoxygenase P450 pathway
A	0019825	molecular_function	oxygen binding
A	0020037	molecular_function	heme binding
A	0031407	biological_process	oxylipin metabolic process
A	0031408	biological_process	oxylipin biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0050832	biological_process	defense response to fungus
B	0004497	molecular_function	monooxygenase activity
B	0005506	molecular_function	iron ion binding
B	0005739	cellular_component	mitochondrion
B	0006629	biological_process	lipid metabolic process
B	0006631	biological_process	fatty acid metabolic process
B	0006633	biological_process	fatty acid biosynthetic process
B	0006952	biological_process	defense response
B	0009507	cellular_component	chloroplast
B	0009534	cellular_component	chloroplast thylakoid
B	0009535	cellular_component	chloroplast thylakoid membrane
B	0009536	cellular_component	plastid
B	0009579	cellular_component	thylakoid
B	0009611	biological_process	response to wounding
B	0009620	biological_process	response to fungus
B	0009695	biological_process	jasmonic acid biosynthetic process
B	0009753	biological_process	response to jasmonic acid
B	0009941	cellular_component	chloroplast envelope
B	0009978	molecular_function	allene oxide synthase activity
B	0010287	cellular_component	plastoglobule
B	0016705	molecular_function	oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
B	0016829	molecular_function	lyase activity
B	0016836	molecular_function	hydro-lyase activity
B	0019373	biological_process	epoxygenase P450 pathway
B	0019825	molecular_function	oxygen binding
B	0020037	molecular_function	heme binding
B	0031407	biological_process	oxylipin metabolic process
B	0031408	biological_process	oxylipin biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0050832	biological_process	defense response to fungus

Functional Information from PDB Data

site_id	AC1
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM A 600

Chain	Residue
A	LYS133
A	THR322
A	GLY325
A	PRO387
A	GLN391
A	TRP455
A	ASN457
A	ASN468
A	LYS469
A	CYS471
A	ALA472
A	LEU137
A	GLY473
A	PHE476
A	HOH603
A	HOH612
A	HOH621
A	HOH622
A	LEU154
A	SER155
A	HIS164
A	LYS168
A	LEU171
A	LEU175
A	ASN321

---

site_id	AC2
Number of Residues	25
Details	BINDING SITE FOR RESIDUE HEM B 600

Chain	Residue
B	LYS133
B	LEU137
B	LEU154
B	SER155
B	HIS164
B	LYS168
B	LEU171
B	ASN321
B	THR322
B	GLY325
B	MET326
B	PRO387
B	GLN391
B	TRP455
B	ASN457
B	ASN468
B	LYS469
B	CYS471
B	ALA472
B	GLY473
B	PHE476
B	HOH610
B	HOH615
B	HOH622
B	HOH624

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL B 1

Chain	Residue
A	GLY366
A	LYS370
B	TYR151
B	SER306
B	GLU309
B	HOH892

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18716621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RCH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RCL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RCM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18716621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RCH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RCL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18716621","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3DSI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"18716621","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RCH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RCL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2RCM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CLI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3DSK","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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