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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: 6BRK
Type: protein
Length: 500 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
UniProt: F8WJE0
Ligands: DGT, MG
Pockets: 3 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 56% helix, 12% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Deoxynucleoside triphosphate triphosphohydrolase SAMHD1	protein	500	56% helix, 12% strand	F8WJE0

Ligands and binding sites

DGT · 2'-deoxyguanosine-5'-triphosphate · ligand · 3 copies · chains A
MG · Magnesium ion · metal

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	803	0.74	0.79	62	DGT
2	162	0.50	0.78	32	empty
3	82	0.43	0.80	21	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

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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