Research workbench
The SAM domain of mouse SAMHD1 is critical for its activation and regulation
Analyse The SAM domain of mouse SAMHD1 is critical for its activation and regulation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6BRH
- Type
- protein
- Length
- 1,002 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
- UniProt
- F8WJE0
- Ligands
- DGT, MG
- Pockets
- 13 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 | protein | 500 | 55% helix, 12% strand | F8WJE0 |
| B | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 | protein | 502 | 55% helix, 12% strand | F8WJE0 |
Ligands and binding sites
- DGT · 2'-deoxyguanosine-5'-triphosphate · ligand · 2 copies · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
13 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 115 | 0.80 | 0.99 | 27 | empty |
| 2 | 964 | 0.75 | 0.78 | 65 | empty |
| 3 | 903 | 0.74 | 0.78 | 71 | empty |
| 4 | 700 | 0.67 | 0.75 | 69 | DGT |
| 5 | 465 | 0.64 | 0.77 | 36 | empty |
Interfaces
1 interface between chains.
- A–B · 1896 Ų buried · 18 hydrogen bonds · protein-protein
Compared structures
- 6BRH · The SAM domain of mouse SAMHD1 is critical for its activation and regulation · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt F8WJE0
- Elsewhere: RCSB PDB 6BRH · PDBe 6BRH · UniProt F8WJE0
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