Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5ISB

Crystal structure of mouse CARM1 in complex with inhibitor SA0435

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0016274	molecular_function	protein-arginine N-methyltransferase activity
A	0018216	biological_process	peptidyl-arginine methylation
B	0016274	molecular_function	protein-arginine N-methyltransferase activity
B	0018216	biological_process	peptidyl-arginine methylation
C	0016274	molecular_function	protein-arginine N-methyltransferase activity
C	0018216	biological_process	peptidyl-arginine methylation
D	0016274	molecular_function	protein-arginine N-methyltransferase activity
D	0018216	biological_process	peptidyl-arginine methylation

Functional Information from PDB Data

site_id	AC1
Number of Residues	26
Details	binding site for residue 6CX A 501

Chain	Residue
A	TYR150
A	ILE198
A	LEU199
A	GLU215
A	ALA216
A	GLY241
A	LYS242
A	VAL243
A	GLU244
A	GLU258
A	MET260
A	PHE151
A	GLU267
A	MET269
A	SER272
A	HOH614
A	HOH624
A	HOH696
A	HOH726
A	TYR154
A	GLN160
A	MET163
A	ARG169
A	GLY193
A	CYS194
A	GLY195

site_id	AC2
Number of Residues	1
Details	binding site for residue EDO A 502

Chain	Residue
A	PHE153

site_id	AC3
Number of Residues	4
Details	binding site for residue EDO A 503

Chain	Residue
A	LYS277
A	LEU280
A	LYS281
A	HOH722

site_id	AC4
Number of Residues	2
Details	binding site for residue EDO A 504

Chain	Residue
A	PHE151
A	LYS242

site_id	AC5
Number of Residues	5
Details	binding site for residue PEG A 505

Chain	Residue
A	LEU178
A	GLN205
D	ASP458
D	THR460
D	GLY461

site_id	AC6
Number of Residues	2
Details	binding site for residue PEG A 506

Chain	Residue
A	TRP404
A	HOH764

site_id	AC7
Number of Residues	5
Details	binding site for residue PEG A 507

Chain	Residue
A	GLN165
A	LEU413
A	THR414
A	HIS415
A	TYR417

site_id	AC8
Number of Residues	2
Details	binding site for residue M2M A 508

Chain	Residue
A	GLY398
A	SER399

site_id	AC9
Number of Residues	26
Details	binding site for residue 6CX B 501

Chain	Residue
B	TYR150
B	PHE151
B	TYR154
B	GLN160
B	MET163
B	ARG169
B	GLY193
B	CYS194
B	ILE198
B	LEU199
B	GLU215
B	ALA216
B	GLY241
B	LYS242
B	VAL243
B	GLU244
B	GLU258
B	MET260
B	GLU267
B	MET269
B	SER272
B	EDO504
B	HOH608
B	HOH635
B	HOH694
B	HOH723

site_id	AD1
Number of Residues	1
Details	binding site for residue EDO B 502

Chain	Residue
B	EDO504

site_id	AD2
Number of Residues	1
Details	binding site for residue EDO B 503

Chain	Residue
B	LEU413

site_id	AD3
Number of Residues	7
Details	binding site for residue EDO B 504

Chain	Residue
B	MET260
B	TYR262
B	GLU267
B	TRP416
B	6CX501
B	EDO502
B	HOH673

site_id	AD4
Number of Residues	1
Details	binding site for residue EDO B 505

Chain	Residue
B	PHE475

site_id	AD5
Number of Residues	2
Details	binding site for residue EDO B 506

Chain	Residue
B	LYS277
B	LEU280

site_id	AD6
Number of Residues	2
Details	binding site for residue PEG B 507

Chain	Residue
B	GLN251
B	TYR279

site_id	AD7
Number of Residues	2
Details	binding site for residue PEG B 508

Chain	Residue
B	TRP404
B	HOH708

site_id	AD8
Number of Residues	27
Details	binding site for residue 6CX C 501

Chain	Residue
C	LEU199
C	GLU215
C	ALA216
C	GLY241
C	LYS242
C	VAL243
C	GLU244
C	GLU258
C	MET260
C	GLU267
C	MET269
C	SER272
C	HOH635
C	HOH645
C	HOH686
C	HOH714
C	HOH739
C	TYR150
C	PHE151
C	TYR154
C	GLN160
C	MET163
C	ARG169
C	GLY193
C	CYS194
C	GLY195
C	ILE198

site_id	AD9
Number of Residues	3
Details	binding site for residue EDO C 503

Chain	Residue
C	TYR417
C	HOH782
C	HOH823

site_id	AE1
Number of Residues	1
Details	binding site for residue EDO C 504

Chain	Residue
C	GLY398

site_id	AE2
Number of Residues	2
Details	binding site for residue EDO C 505

Chain	Residue
C	LEU178
C	PEG506

site_id	AE3
Number of Residues	4
Details	binding site for residue PEG C 506

Chain	Residue
B	THR460
C	LEU178
C	GLN205
C	EDO505

site_id	AE4
Number of Residues	8
Details	binding site for residue PG4 C 507

Chain	Residue
C	LYS277
C	LEU280
C	LYS281
C	PRO282
C	LEU361
C	HOH747
C	HOH750
C	HOH812

site_id	AE5
Number of Residues	26
Details	binding site for residue 6CX D 501

Chain	Residue
D	PHE151
D	TYR154
D	GLN160
D	MET163
D	ARG169
D	GLY193
D	CYS194
D	GLY195
D	ILE198
D	LEU199
D	GLU215
D	ALA216
D	GLY241
D	LYS242
D	VAL243
D	GLU244
D	GLU258
D	PRO259
D	MET260
D	GLU267
D	MET269
D	SER272
D	HOH615
D	HOH632
D	HOH658
D	HOH700

site_id	AE6
Number of Residues	2
Details	binding site for residue EDO D 502

Chain	Residue
D	ASP393
D	TRP404

site_id	AE7
Number of Residues	2
Details	binding site for residue EDO D 503

Chain	Residue
D	GLN251
D	TYR279

site_id	AE8
Number of Residues	4
Details	binding site for residue EDO D 505

Chain	Residue
D	THR299
D	ASP300
D	GLU301
D	HOH755

site_id	AE9
Number of Residues	4
Details	binding site for residue PEG D 506

Chain	Residue
D	ASN162
D	LEU413
D	HIS415
D	TYR417

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	24
Details	BINDING: BINDING => ECO:0000269\|PubMed:17882261

Chain	Residue	Details
A	GLN160
B	GLU215
B	GLU244
B	SER272
C	GLN160
C	ARG169
C	GLY193
C	GLU215
C	GLU244
C	SER272
D	GLN160
A	ARG169
D	ARG169
D	GLY193
D	GLU215
D	GLU244
D	SER272
A	GLY193
A	GLU215
A	GLU244
A	SER272
B	GLN160
B	ARG169
B	GLY193

site_id	SWS_FT_FI2
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:19843527

Chain	Residue	Details
A	SER217
B	SER217
C	SER217
D	SER217

site_id	SWS_FT_FI3
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250\|UniProtKB:Q86X55

Chain	Residue	Details
A	LYS228
B	LYS228
C	LYS228
D	LYS228

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