MolNFT v1 · #144376 · protein
The SAM domain of mouse SAMHD1 is critical for its activation and regulation
6BRK: “The SAM domain of mouse SAMHD1 is critical for its activation and regulation”. X-ray diffraction, 2 ligands (DGT, MG). MolNFT v1 #144376 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6BRK
- Type
- protein
- Length
- 500 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- F8WJE0
- Ligands
- DGT, MG
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 500 | — | F8WJE0 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6BRK · 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 6BRK · PDBe 6BRK · UniProt F8WJE0
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