4X60

Crystal structure of PRMT5:MEP50 with EPZ015666 and sinefungin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000387	biological_process	spliceosomal snRNP assembly
A	0000785	cellular_component	chromatin
A	0002039	molecular_function	p53 binding
A	0003714	molecular_function	transcription corepressor activity
A	0005515	molecular_function	protein binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0005737	cellular_component	cytoplasm
A	0005794	cellular_component	Golgi apparatus
A	0005829	cellular_component	cytosol
A	0006325	biological_process	chromatin organization
A	0006338	biological_process	chromatin remodeling
A	0006353	biological_process	DNA-templated transcription termination
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006479	biological_process	protein methylation
A	0007088	biological_process	regulation of mitotic nuclear division
A	0008168	molecular_function	methyltransferase activity
A	0008327	molecular_function	methyl-CpG binding
A	0008469	molecular_function	histone arginine N-methyltransferase activity
A	0010468	biological_process	regulation of gene expression
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	0032922	biological_process	circadian regulation of gene expression
A	0032991	cellular_component	protein-containing complex
A	0034709	cellular_component	methylosome
A	0035097	cellular_component	histone methyltransferase complex
A	0035243	molecular_function	protein-arginine omega-N symmetric methyltransferase activity
A	0035246	biological_process	peptidyl-arginine N-methylation
A	0042054	molecular_function	histone methyltransferase activity
A	0042118	biological_process	endothelial cell activation
A	0042802	molecular_function	identical protein binding
A	0043021	molecular_function	ribonucleoprotein complex binding
A	0044020	molecular_function	histone H4R3 methyltransferase activity
A	0044027	biological_process	negative regulation of gene expression via chromosomal CpG island methylation
A	0044877	molecular_function	protein-containing complex binding
A	0045596	biological_process	negative regulation of cell differentiation
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0046982	molecular_function	protein heterodimerization activity
A	0048026	biological_process	positive regulation of mRNA splicing, via spliceosome
A	0048511	biological_process	rhythmic process
A	0048714	biological_process	positive regulation of oligodendrocyte differentiation
A	0070372	biological_process	regulation of ERK1 and ERK2 cascade
A	0070888	molecular_function	E-box binding
A	0090161	biological_process	Golgi ribbon formation
A	0097421	biological_process	liver regeneration
A	0140938	molecular_function	histone H3 methyltransferase activity
A	1901796	biological_process	regulation of signal transduction by p53 class mediator
A	1904992	biological_process	positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway
B	0000209	biological_process	protein polyubiquitination
B	0000387	biological_process	spliceosomal snRNP assembly
B	0003713	molecular_function	transcription coactivator activity
B	0005515	molecular_function	protein binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005794	cellular_component	Golgi apparatus
B	0005829	cellular_component	cytosol
B	0006357	biological_process	regulation of transcription by RNA polymerase II
B	0006511	biological_process	ubiquitin-dependent protein catabolic process
B	0007309	biological_process	oocyte axis specification
B	0008284	biological_process	positive regulation of cell population proliferation
B	0008285	biological_process	negative regulation of cell population proliferation
B	0008327	molecular_function	methyl-CpG binding
B	0031465	cellular_component	Cul4B-RING E3 ubiquitin ligase complex
B	0034709	cellular_component	methylosome
B	0045893	biological_process	positive regulation of DNA-templated transcription
B	0048026	biological_process	positive regulation of mRNA splicing, via spliceosome
B	0060528	biological_process	secretory columnal luminar epithelial cell differentiation involved in prostate glandular acinus development
B	0060767	biological_process	epithelial cell proliferation involved in prostate gland development
B	0060770	biological_process	negative regulation of epithelial cell proliferation involved in prostate gland development
B	1990234	cellular_component	transferase complex
B	1990756	molecular_function	ubiquitin-like ligase-substrate adaptor activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	19
Details	binding site for residue SFG A 701

Chain	Residue
A	LEU315
A	SER418
A	ASP419
A	MET420
A	GLU435
A	LEU436
A	CYS449
A	3XV702
A	HOH819
A	HOH820
A	HOH904
A	TYR324
A	LYS333
A	TYR334
A	GLY365
A	GLY367
A	PRO370
A	GLU392
A	LYS393

---

site_id	AC2
Number of Residues	15
Details	binding site for residue 3XV A 702

Chain	Residue
A	GLN309
A	LEU319
A	PHE327
A	LYS333
A	GLU435
A	LEU437
A	SER439
A	GLU444
A	VAL503
A	PHE577
A	SER578
A	TRP579
A	PHE580
A	SFG701
A	HOH817

---

site_id	AC3
Number of Residues	3
Details	binding site for residue GOL A 703

Chain	Residue
A	PHE40
A	THR80
A	GLN263

---

site_id	AC4
Number of Residues	7
Details	binding site for residue GOL A 704

Chain	Residue
A	ARG52
A	GLU53
A	PHE54
A	LYS60
A	GLN66
A	GLN109
A	HOH908

---

site_id	AC5
Number of Residues	2
Details	binding site for residue GOL A 705

Chain	Residue
A	TYR297
A	GLY575

---

Functional Information from PROSITE/UniProt

site_id	PS00678
Number of Residues	15
Details	WD_REPEATS_1 Trp-Asp (WD) repeats signature. AVSGskDiCIKVWDL

Chain	Residue	Details
B	ALA140-LEU154

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	307
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	279
Details	Region: {"description":"TIM barrel","evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	172
Details	Region: {"description":"Beta barrel","evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Region: {"description":"Dimerization","evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Active site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Site: {"description":"Critical for specifying symmetric addition of methyl groups","evidences":[{"source":"UniProtKB","id":"P46580","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	53
Details	Repeat: {"description":"WD 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI9
Number of Residues	38
Details	Repeat: {"description":"WD 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI10
Number of Residues	39
Details	Repeat: {"description":"WD 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	40
Details	Repeat: {"description":"WD 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI12
Number of Residues	41
Details	Repeat: {"description":"WD 5","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI13
Number of Residues	40
Details	Repeat: {"description":"WD 6","evidences":[{"source":"PROSITE-ProRule","id":"PRU00221","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23071334","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---