MolNFT v1 · #113729 · protein
Crystal structure of human SAMHD1 (amino acid residues 115-626) bound to GTP
5AO3 · Deoxynucleoside triphosphate triphosphohydrolase SAMHD1: “Crystal structure of human SAMHD1 (amino acid residues 115-626) bound to GTP”. X-ray diffraction, 3 ligands (GTP, FE, SO4), 20 pockets (best druggability 0.83). MolNFT v1…
- PDB
- 5AO3
- Type
- protein
- Length
- 1,756 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
- EC
- 3.1.5.-
- UniProt
- Q9Y3Z3
- Ligands
- GTP, FE, SO4
- Pockets
- 20 · best druggability 0.83
Structure
x-ray diffraction · 4 distinct chains · 52% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (EC 3.1.5.-) | protein | 440 | 51% helix, 12% strand | Q9Y3Z3 |
| B | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (EC 3.1.5.-) | protein | 438 | 54% helix, 12% strand | Q9Y3Z3 |
| C | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (EC 3.1.5.-) | protein | 439 | 52% helix, 12% strand | Q9Y3Z3 |
| D | Deoxynucleoside triphosphate triphosphohydrolase SAMHD1 (EC 3.1.5.-) | protein | 439 | 52% helix, 13% strand | Q9Y3Z3 |
Ligands and binding sites
- GTP · Guanosine-5'-triphosphate · ligand · 4 copies · chains A, C, B, D
- FE · Fe (III) ion · metal · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 11 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.83 | 0.98 | 28 | empty |
| 2 | 172 | 0.83 | 0.98 | 26 | empty |
| 3 | 720 | 0.78 | 0.82 | 66 | SO4 |
| 4 | 637 | 0.78 | 0.83 | 55 | SO4 |
| 5 | 726 | 0.77 | 0.82 | 67 | FE, SO4 |
Interfaces
3 interfaces between chains.
- A–C · 1900 Ų buried · 21 hydrogen bonds · protein-protein
- B–D · 1869 Ų buried · 23 hydrogen bonds · protein-protein
- A–B · 488 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
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 5AO3 · PDBe 5AO3 · UniProt Q9Y3Z3
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