6BRK

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue DGT A 701

Chain	Residue
A	LEU182
A	TYR347
A	ASP351
A	TYR417
A	ARG196
A	ARG238
A	ASN239
A	HIS242
A	HIS247
A	HIS265
A	GLU266
A	ASP343

---

site_id	AC2
Number of Residues	11
Details	binding site for residue DGT A 702

Chain	Residue
A	VAL149
A	ASN151
A	HIS157
A	VAL188
A	PHE189
A	ARG395
A	ARG415
A	HIS419
A	LYS420
A	MG703
A	DGT704

---

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

Chain	Residue
A	LYS148
A	DGT702
A	DGT704

---

site_id	AC4
Number of Residues	14
Details	binding site for residue DGT A 704

Chain	Residue
A	ARG75
A	LYS148
A	VAL149
A	PHE150
A	ASP169
A	GLN174
A	ARG177
A	TYR187
A	VAL188
A	PHE197
A	ILE421
A	ARG494
A	DGT702
A	MG703

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	65
Details	Domain: {"description":"SAM","evidences":[{"source":"PROSITE-ProRule","id":"PRU00184","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	1
Details	Active site: {"evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	5
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	1
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	7
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	4
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	4
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI8
Number of Residues	4
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	1
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	1
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Y3Z3","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI11
Number of Residues	2
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

---