MolNFT v1 · #144372 · protein
The SAM domain of mouse SAMHD1 is critical for its activation and regulation
6BRG: “The SAM domain of mouse SAMHD1 is critical for its activation and regulation”. X-ray diffraction, 1 ligand (MG). MolNFT v1 #144372 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6BRG
- Type
- protein
- Length
- 2,000 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F8WJE0
- Ligands
- MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 500 | — | F8WJE0 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6BRG · 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 6BRG · PDBe 6BRG · UniProt F8WJE0
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