MolNFT v1 · #146895 · protein
SAMHD1 bound to cladribine-tp in the catalytic pocket and allosteric pocket
6DW4: “SAMHD1 bound to cladribine-tp in the catalytic pocket and allosteric pocket”. X-ray diffraction, 4 ligands (HF7, GTP, MG). MolNFT v1 #146895 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6DW4
- Type
- protein
- Length
- 1,924 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9Y3Z3
- Ligands
- HF7, GTP, MG, NA
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, C, B, A | — | protein | 481 | — | Q9Y3Z3 |
Ligands and binding sites
- HF7 · 2'-deoxy-2-methyladenosine 5'-(tetrahydrogen triphosphate) · ligand · 8 copies · chains D, C, B, A
- GTP · Guanosine-5'-triphosphate · ligand · 4 copies · chains D, C, A, B
- MG · Magnesium ion · metal · 8 copies · chains D, C, B, A
- NA · Sodium ion · metal · chains C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6DW4 · SAMHD1 Bound to Cladribine-TP in the Catalytic Pocket and Allosteric Pocket · the same entry in another collection · chain D against D, 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 Q9Y3Z3
- Elsewhere: RCSB PDB 6DW4 · PDBe 6DW4 · UniProt Q9Y3Z3
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