3B3F

The 2.2 A crystal structure of the catalytic domain of coactivator-associated arginine methyl transferase I(CARM1,142-478), in complex with S-adenosyl homocysteine

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	24
Details	BINDING SITE FOR RESIDUE SAH A 481

Chain	Residue
A	TYR150
A	ILE198
A	LEU199
A	GLU215
A	ALA216
A	GLY241
A	LYS242
A	VAL243
A	GLU244
A	GLU258
A	MET269
A	PHE151
A	SER272
A	HOH484
A	HOH492
A	HOH631
A	HOH632
A	TYR154
A	GLN160
A	MET163
A	ARG169
A	GLY193
A	CYS194
A	GLY195

---

site_id	AC2
Number of Residues	23
Details	BINDING SITE FOR RESIDUE SAH B 481

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	MET269
B	SER272
B	HOH486
B	HOH497
B	HOH610
B	HOH611

---

site_id	AC3
Number of Residues	22
Details	BINDING SITE FOR RESIDUE SAH C 481

Chain	Residue
C	TYR150
C	PHE151
C	TYR154
C	GLN160
C	MET163
C	ARG169
C	GLY193
C	CYS194
C	ILE198
C	LEU199
C	GLU215
C	ALA216
C	GLY241
C	LYS242
C	VAL243
C	GLU244
C	GLU258
C	MET269
C	SER272
C	HOH498
C	HOH515
C	HOH547

---

site_id	AC4
Number of Residues	23
Details	BINDING SITE FOR RESIDUE SAH D 481

Chain	Residue
D	TYR150
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	MET269
D	SER272
D	HOH482
D	HOH483
D	HOH489
D	HOH544

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1228
Details	Domain: {"description":"SAM-dependent MTase PRMT-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01015","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	132
Details	Region: {"description":"Required for nuclear translocation","evidences":[{"source":"UniProtKB","id":"Q9WVG6","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	24
Details	Binding site: {"evidences":[{"source":"PubMed","id":"17882262","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q86X55","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q86X55","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1or8

Chain	Residue	Details
A	GLU258
A	GLU267

---

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1or8

Chain	Residue	Details
B	GLU258
B	GLU267

---

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1or8

Chain	Residue	Details
C	GLU258
C	GLU267

---

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1or8

Chain	Residue	Details
D	GLU258
D	GLU267

---