6BRH
The SAM domain of mouse SAMHD1 is critical for its activation and regulation
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000724 | biological_process | double-strand break repair via homologous recombination |
| A | 0003676 | molecular_function | nucleic acid binding |
| A | 0003697 | molecular_function | single-stranded DNA binding |
| A | 0003723 | molecular_function | RNA binding |
| A | 0004540 | molecular_function | RNA nuclease activity |
| 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 | 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 | 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 | 0045088 | biological_process | regulation of innate immune response |
| A | 0046061 | biological_process | dATP catabolic process |
| 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 | 0000724 | biological_process | double-strand break repair via homologous recombination |
| B | 0003676 | molecular_function | nucleic acid binding |
| B | 0003697 | molecular_function | single-stranded DNA binding |
| B | 0003723 | molecular_function | RNA binding |
| B | 0004540 | molecular_function | RNA nuclease activity |
| 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 | 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 | 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 | 0045088 | biological_process | regulation of innate immune response |
| B | 0046061 | biological_process | dATP catabolic process |
| 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 |
