2J5C

Rational conversion of substrate and product specificity in a monoterpene synthase. Structural insights into the molecular basis of rapid evolution.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0009507	cellular_component	chloroplast
A	0009536	cellular_component	plastid
A	0010333	molecular_function	terpene synthase activity
A	0010597	biological_process	green leaf volatile biosynthetic process
A	0016099	biological_process	monoterpenoid biosynthetic process
A	0016102	biological_process	diterpenoid biosynthetic process
A	0016114	biological_process	terpenoid biosynthetic process
A	0016829	molecular_function	lyase activity
A	0016838	molecular_function	carbon-oxygen lyase activity, acting on phosphates
A	0046248	biological_process	alpha-pinene biosynthetic process
A	0046872	molecular_function	metal ion binding
A	0050550	molecular_function	pinene synthase activity
A	0050551	molecular_function	myrcene synthase activity
A	0080015	molecular_function	sabinene synthase activity
A	0102313	molecular_function	1,8-cineole synthase activity
B	0000287	molecular_function	magnesium ion binding
B	0009507	cellular_component	chloroplast
B	0009536	cellular_component	plastid
B	0010333	molecular_function	terpene synthase activity
B	0010597	biological_process	green leaf volatile biosynthetic process
B	0016099	biological_process	monoterpenoid biosynthetic process
B	0016102	biological_process	diterpenoid biosynthetic process
B	0016114	biological_process	terpenoid biosynthetic process
B	0016829	molecular_function	lyase activity
B	0016838	molecular_function	carbon-oxygen lyase activity, acting on phosphates
B	0046248	biological_process	alpha-pinene biosynthetic process
B	0046872	molecular_function	metal ion binding
B	0050550	molecular_function	pinene synthase activity
B	0050551	molecular_function	myrcene synthase activity
B	0080015	molecular_function	sabinene synthase activity
B	0102313	molecular_function	1,8-cineole synthase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE BME A1592

Chain	Residue
A	CYS122
A	HIS123

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site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE BME A1593

Chain	Residue
A	ARG310
A	GLU313
A	CYS314
A	ASN338
A	THR342

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site_id	AC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE BME B1592

Chain	Residue
B	ARG325
B	CYS122
B	HIS123

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site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE BME B1593

Chain	Residue
B	ARG310
B	GLU313
B	CYS314
B	ASN338
B	ALA339
B	THR342
B	HOH2107

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	14
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q40577

Chain	Residue	Details
A	ARG308
B	ASP349
B	ARG486
B	ASP489
B	THR493
B	GLU497
A	ASP345
A	ASP349
A	ARG486
A	ASP489
A	THR493
A	GLU497
B	ARG308
B	ASP345

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Confers catalytic properties (activation of water molecule and hydroxylation of the alpha-terpinyl cation) => ECO:0000269|PubMed:17557809

Chain	Residue	Details
A	ASN338
B	ASN338

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1n20

Chain	Residue	Details
A	TRP317
A	PHE571

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1n20

Chain	Residue	Details
B	TRP317
B	PHE571

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