Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6BRH

The SAM domain of mouse SAMHD1 is critical for its activation and regulation

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000724	biological_process	double-strand break repair via homologous recombination
A	0002376	biological_process	immune system process
A	0003676	molecular_function	nucleic acid binding
A	0003697	molecular_function	single-stranded DNA binding
A	0003723	molecular_function	RNA binding
A	0003824	molecular_function	catalytic activity
A	0004540	molecular_function	RNA nuclease activity
A	0005525	molecular_function	GTP binding
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005694	cellular_component	chromosome
A	0005886	cellular_component	plasma membrane
A	0006203	biological_process	dGTP catabolic process
A	0006260	biological_process	DNA replication
A	0006281	biological_process	DNA repair
A	0006974	biological_process	DNA damage response
A	0008270	molecular_function	zinc ion binding
A	0008832	molecular_function	dGTPase activity
A	0009264	biological_process	deoxyribonucleotide catabolic process
A	0016446	biological_process	somatic hypermutation of immunoglobulin genes
A	0016787	molecular_function	hydrolase activity
A	0016793	molecular_function	triphosphoric monoester hydrolase activity
A	0032567	molecular_function	dGTP binding
A	0035861	cellular_component	site of double-strand break
A	0042802	molecular_function	identical protein binding
A	0045087	biological_process	innate immune response
A	0045088	biological_process	regulation of innate immune response
A	0046061	biological_process	dATP catabolic process
A	0046872	molecular_function	metal ion binding
A	0051289	biological_process	protein homotetramerization
A	0051607	biological_process	defense response to virus
A	0060339	biological_process	negative regulation of type I interferon-mediated signaling pathway
A	0097197	cellular_component	tetraspanin-enriched microdomain
A	0106375	molecular_function	deoxynucleoside triphosphate hydrolase activity
A	0110025	biological_process	DNA strand resection involved in replication fork processing
B	0000166	molecular_function	nucleotide binding
B	0000724	biological_process	double-strand break repair via homologous recombination
B	0002376	biological_process	immune system process
B	0003676	molecular_function	nucleic acid binding
B	0003697	molecular_function	single-stranded DNA binding
B	0003723	molecular_function	RNA binding
B	0003824	molecular_function	catalytic activity
B	0004540	molecular_function	RNA nuclease activity
B	0005525	molecular_function	GTP binding
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005694	cellular_component	chromosome
B	0005886	cellular_component	plasma membrane
B	0006203	biological_process	dGTP catabolic process
B	0006260	biological_process	DNA replication
B	0006281	biological_process	DNA repair
B	0006974	biological_process	DNA damage response
B	0008270	molecular_function	zinc ion binding
B	0008832	molecular_function	dGTPase activity
B	0009264	biological_process	deoxyribonucleotide catabolic process
B	0016446	biological_process	somatic hypermutation of immunoglobulin genes
B	0016787	molecular_function	hydrolase activity
B	0016793	molecular_function	triphosphoric monoester hydrolase activity
B	0032567	molecular_function	dGTP binding
B	0035861	cellular_component	site of double-strand break
B	0042802	molecular_function	identical protein binding
B	0045087	biological_process	innate immune response
B	0045088	biological_process	regulation of innate immune response
B	0046061	biological_process	dATP catabolic process
B	0046872	molecular_function	metal ion binding
B	0051289	biological_process	protein homotetramerization
B	0051607	biological_process	defense response to virus
B	0060339	biological_process	negative regulation of type I interferon-mediated signaling pathway
B	0097197	cellular_component	tetraspanin-enriched microdomain
B	0106375	molecular_function	deoxynucleoside triphosphate hydrolase activity
B	0110025	biological_process	DNA strand resection involved in replication fork processing

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 701

Chain	Residue
A	ARG196
A	HIS199
A	HIS238
A	ASP239
A	ASP343
A	HOH804

site_id	AC2
Number of Residues	13
Details	binding site for residue DGT A 702

Chain	Residue
A	PHE150
A	ASP169
A	GLN174
A	ARG177
A	PHE197
B	TYR187
B	VAL188
B	LYS420
B	ILE421
B	ARG494
A	ARG75
A	LYS148
A	VAL149

site_id	AC3
Number of Residues	13
Details	binding site for residue DGT B 701

Chain	Residue
A	TYR187
A	VAL188
A	LYS420
A	ILE421
A	ARG494
B	ARG75
B	LYS148
B	VAL149
B	PHE150
B	ASP169
B	GLN174
B	ARG177
B	PHE197

site_id	AC4
Number of Residues	6
Details	binding site for residue MG B 702

Chain	Residue
B	ARG196
B	HIS199
B	HIS238
B	ASP239
B	ASP343
B	HOH801

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	130
Details	Domain: {"description":"SAM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00184","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	2
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	10
Details	Binding site: {"description":"in chain B","evidences":[{"source":"PubMed","id":"29379009","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6BRH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	2
Details	Binding site: {"description":"in chain B","evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	14
Details	Binding site: {"evidences":[{"source":"PubMed","id":"29379009","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BRH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"description":"in chain C","evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Binding site: {"description":"in chain A","evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Binding site: {"description":"in chain C","evidences":[{"source":"PubMed","id":"29379009","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6BRH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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