Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3P9K

Crystal structure of perennial ryegrass LpOMT1 complexed with S-adenosyl-L-homocysteine and coniferaldehyde

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0008168	molecular_function	methyltransferase activity
A	0008171	molecular_function	O-methyltransferase activity
A	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
A	0016206	molecular_function	catechol O-methyltransferase activity
A	0016740	molecular_function	transferase activity
A	0019438	biological_process	aromatic compound biosynthetic process
A	0032259	biological_process	methylation
A	0046983	molecular_function	protein dimerization activity
A	0102084	molecular_function	obsolete L-dopa O-methyltransferase activity
A	0102938	molecular_function	obsolete orcinol O-methyltransferase activity
B	0003824	molecular_function	catalytic activity
B	0008168	molecular_function	methyltransferase activity
B	0008171	molecular_function	O-methyltransferase activity
B	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
B	0016206	molecular_function	catechol O-methyltransferase activity
B	0016740	molecular_function	transferase activity
B	0019438	biological_process	aromatic compound biosynthetic process
B	0032259	biological_process	methylation
B	0046983	molecular_function	protein dimerization activity
B	0102084	molecular_function	obsolete L-dopa O-methyltransferase activity
B	0102938	molecular_function	obsolete orcinol O-methyltransferase activity
C	0003824	molecular_function	catalytic activity
C	0008168	molecular_function	methyltransferase activity
C	0008171	molecular_function	O-methyltransferase activity
C	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
C	0016206	molecular_function	catechol O-methyltransferase activity
C	0016740	molecular_function	transferase activity
C	0019438	biological_process	aromatic compound biosynthetic process
C	0032259	biological_process	methylation
C	0046983	molecular_function	protein dimerization activity
C	0102084	molecular_function	obsolete L-dopa O-methyltransferase activity
C	0102938	molecular_function	obsolete orcinol O-methyltransferase activity
D	0003824	molecular_function	catalytic activity
D	0008168	molecular_function	methyltransferase activity
D	0008171	molecular_function	O-methyltransferase activity
D	0008757	molecular_function	S-adenosylmethionine-dependent methyltransferase activity
D	0016206	molecular_function	catechol O-methyltransferase activity
D	0016740	molecular_function	transferase activity
D	0019438	biological_process	aromatic compound biosynthetic process
D	0032259	biological_process	methylation
D	0046983	molecular_function	protein dimerization activity
D	0102084	molecular_function	obsolete L-dopa O-methyltransferase activity
D	0102938	molecular_function	obsolete orcinol O-methyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	BINDING SITE FOR RESIDUE SAH A 401

Chain	Residue
A	MET177
A	PHE250
A	LYS262
A	ILE264
A	ASP267
A	CIY601
A	HOH1027
A	HOH1054
A	HOH1199
A	HOH1203
A	HOH1331
A	SER181
A	GLY205
A	GLY207
A	ASP228
A	LEU229
A	VAL232
A	ASP248
A	MET249

site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SAH B 402

Chain	Residue
B	MET177
B	SER181
B	GLY205
B	GLY207
B	ASP228
B	LEU229
B	VAL232
B	GLY247
B	ASP248
B	MET249
B	LYS262
B	ILE264
B	ASP267
B	CIY602
B	HOH1067
B	HOH1183
B	HOH1205

site_id	AC3
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SAH C 403

Chain	Residue
C	MET177
C	SER181
C	GLY205
C	GLY207
C	ASP228
C	LEU229
C	ASP248
C	MET249
C	LYS262
C	ASP267
C	CIY603
C	HOH1003
C	HOH1036
C	HOH1245
C	HOH1261
C	HOH1324
C	HOH1637

site_id	AC4
Number of Residues	17
Details	BINDING SITE FOR RESIDUE SAH D 404

Chain	Residue
D	PHE160
D	MET177
D	SER181
D	GLY205
D	GLY207
D	ASP228
D	VAL232
D	ASP248
D	MET249
D	PHE250
D	LYS262
D	ASP267
D	CIY604
D	HOH1017
D	HOH1049
D	HOH1338
D	HOH1395

site_id	AC5
Number of Residues	12
Details	BINDING SITE FOR RESIDUE CIY A 601

Chain	Residue
A	MET127
A	ASN128
A	MET177
A	TRP263
A	HIS266
A	ASP267
A	ILE316
A	MET317
A	ASN321
A	SAH401
A	HOH1101
B	SER25

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE CIY B 602

Chain	Residue
B	MET127
B	ASN128
B	PHE173
B	TRP263
B	HIS266
B	ASP267
B	MET317
B	ASN321
B	SAH402
B	HOH1115

site_id	AC7
Number of Residues	9
Details	BINDING SITE FOR RESIDUE CIY C 603

Chain	Residue
C	SAH403
C	HOH1062
C	MET127
C	ASN128
C	TRP263
C	HIS266
C	ASP267
C	MET317
C	ASN321

site_id	AC8
Number of Residues	11
Details	BINDING SITE FOR RESIDUE CIY D 604

Chain	Residue
D	MET127
D	ASN128
D	PHE173
D	TRP263
D	HIS266
D	ASP267
D	MET317
D	ASN321
D	SAH404
D	HOH1089
D	HOH1480

Functional Information from PROSITE/UniProt

site_id	PS00012
Number of Residues	16
Details	PHOSPHOPANTETHEINE Phosphopantetheine attachment site. AAGGKSLTPTEVAAKL

Chain	Residue	Details
A	ALA47-LEU62

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)