6BRK
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 | 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 | 1 |
| Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:Q9Y3Z3 |
| Chain | Residue | Details |
| A | HIS265 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 5 |
| Details | BINDING: in chain B => ECO:0000305|PubMed:29379009, ECO:0007744|PDB:6BRH |
| Chain | Residue | Details |
| A | LYS148 | |
| A | VAL149 | |
| A | ASP169 | |
| A | GLN174 | |
| A | ARG177 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: in chain B => ECO:0000250|UniProtKB:Q9Y3Z3 |
| Chain | Residue | Details |
| A | ASN151 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:29379009, ECO:0007744|PDB:6BRH |
| Chain | Residue | Details |
| A | LEU182 | |
| A | HIS247 | |
| A | HIS265 | |
| A | GLU266 | |
| A | TYR347 | |
| A | ASP351 | |
| A | TYR417 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: in chain C => ECO:0000250|UniProtKB:Q9Y3Z3 |
| Chain | Residue | Details |
| A | VAL188 | |
| A | HIS419 | |
| A | LYS420 | |
| A | LYS498 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9Y3Z3 |
| Chain | Residue | Details |
| A | HIS199 | |
| A | ARG238 | |
| A | ASN239 | |
| A | ASP343 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 5 |
| Details | BINDING: in chain A => ECO:0000250|UniProtKB:Q9Y3Z3 |
| Chain | Residue | Details |
| A | ARG365 | |
| A | ARG395 | |
| A | LYS397 | |
| A | ASN401 | |
| A | LYS565 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: in chain C => ECO:0000305|PubMed:29379009, ECO:0007744|PDB:6BRH |
| Chain | Residue | Details |
| A | ARG494 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | SER49 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | THR52 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | SER55 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | THR56 |
| site_id | SWS_FT_FI13 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9Y3Z3 |
| Chain | Residue | Details |
| A | SER64 | |
| A | SER125 |
| site_id | SWS_FT_FI14 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:26667483, ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079 |
| Chain | Residue | Details |
| A | THR634 |
| site_id | SWS_FT_FI15 |
| Number of Residues | 2 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250|UniProtKB:Q9Y3Z3 |
| Chain | Residue | Details |
| A | LYS509 |
