Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6CU3

Crystal structure of a protein arginine N-methyltransferase from Naegleria fowleri

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005634	cellular_component	nucleus
A	0006338	biological_process	chromatin remodeling
A	0008168	molecular_function	methyltransferase activity
A	0016274	molecular_function	protein-arginine N-methyltransferase activity
A	0016740	molecular_function	transferase activity
A	0018216	biological_process	peptidyl-arginine methylation
A	0032259	biological_process	methylation
A	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
A	0042054	molecular_function	histone methyltransferase activity
B	0005634	cellular_component	nucleus
B	0006338	biological_process	chromatin remodeling
B	0008168	molecular_function	methyltransferase activity
B	0016274	molecular_function	protein-arginine N-methyltransferase activity
B	0016740	molecular_function	transferase activity
B	0018216	biological_process	peptidyl-arginine methylation
B	0032259	biological_process	methylation
B	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
B	0042054	molecular_function	histone methyltransferase activity
C	0005634	cellular_component	nucleus
C	0006338	biological_process	chromatin remodeling
C	0008168	molecular_function	methyltransferase activity
C	0016274	molecular_function	protein-arginine N-methyltransferase activity
C	0016740	molecular_function	transferase activity
C	0018216	biological_process	peptidyl-arginine methylation
C	0032259	biological_process	methylation
C	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
C	0042054	molecular_function	histone methyltransferase activity
D	0005634	cellular_component	nucleus
D	0006338	biological_process	chromatin remodeling
D	0008168	molecular_function	methyltransferase activity
D	0016274	molecular_function	protein-arginine N-methyltransferase activity
D	0016740	molecular_function	transferase activity
D	0018216	biological_process	peptidyl-arginine methylation
D	0032259	biological_process	methylation
D	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
D	0042054	molecular_function	histone methyltransferase activity
E	0005634	cellular_component	nucleus
E	0006338	biological_process	chromatin remodeling
E	0008168	molecular_function	methyltransferase activity
E	0016274	molecular_function	protein-arginine N-methyltransferase activity
E	0016740	molecular_function	transferase activity
E	0018216	biological_process	peptidyl-arginine methylation
E	0032259	biological_process	methylation
E	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
E	0042054	molecular_function	histone methyltransferase activity
F	0005634	cellular_component	nucleus
F	0006338	biological_process	chromatin remodeling
F	0008168	molecular_function	methyltransferase activity
F	0016274	molecular_function	protein-arginine N-methyltransferase activity
F	0016740	molecular_function	transferase activity
F	0018216	biological_process	peptidyl-arginine methylation
F	0032259	biological_process	methylation
F	0035242	molecular_function	protein-arginine omega-N asymmetric methyltransferase activity
F	0042054	molecular_function	histone methyltransferase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	binding site for residue EDO A 401

Chain	Residue
A	ARG82
A	LYS98

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO A 402

Chain	Residue
A	LYS45
A	ASP115
A	PRO145
E	ASP44

site_id	AC3
Number of Residues	3
Details	binding site for residue EDO A 403

Chain	Residue
A	THR155
A	LYS209
A	GLU212

site_id	AC4
Number of Residues	5
Details	binding site for residue EDO A 404

Chain	Residue
A	ASP163
A	TYR166
A	ASP196
A	GLN202
A	TYR278

site_id	AC5
Number of Residues	3
Details	binding site for residue EDO A 405

Chain	Residue
A	THR206
A	GLN235
A	ASN288

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO B 401

Chain	Residue
B	LEU22
B	LYS23
B	ASP24
B	ARG27
B	THR28

site_id	AC7
Number of Residues	2
Details	binding site for residue EDO B 402

Chain	Residue
B	ARG82
B	LYS98

site_id	AC8
Number of Residues	6
Details	binding site for residue EDO B 403

Chain	Residue
B	ASP44
B	LYS45
B	ASP115
B	ARG144
B	PRO145
B	TYR148

site_id	AC9
Number of Residues	4
Details	binding site for residue EDO B 404

Chain	Residue
B	GLY123
B	TYR124
B	HIS271
B	TRP272

site_id	AD1
Number of Residues	3
Details	binding site for residue EDO B 405

Chain	Residue
B	LEU223
B	ILE226
B	GLN299

site_id	AD2
Number of Residues	3
Details	binding site for residue EDO C 401

Chain	Residue
C	TYR239
E	GLN237
E	TYR239

site_id	AD3
Number of Residues	2
Details	binding site for residue EDO E 401

Chain	Residue
E	ARG82
E	LYS98

site_id	AD4
Number of Residues	4
Details	binding site for residue EDO E 402

Chain	Residue
E	MET122
E	TYR124
E	HIS271
E	TRP272

site_id	AD5
Number of Residues	3
Details	binding site for residue EDO E 403

Chain	Residue
E	ASP175
E	ASN176
E	GLY179

site_id	AD6
Number of Residues	3
Details	binding site for residue EDO E 404

Chain	Residue
E	GLU192
E	ARG328
E	EDO405

site_id	AD7
Number of Residues	4
Details	binding site for residue EDO E 405

Chain	Residue
E	TYR124
E	VAL195
E	LYS273
E	EDO404

site_id	AD8
Number of Residues	2
Details	binding site for residue EDO E 406

Chain	Residue
E	LEU223
E	GLN299

site_id	AD9
Number of Residues	3
Details	binding site for residue EDO E 407

Chain	Residue
E	LEU283
E	PRO284
E	VAL315

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