MolNFT v1 · #11370 · protein
Solution structure of the nudix enzyme diadenosine tetraphosphate hydrolase from lupinus angustifolius complexed with ATP
1JKN · Diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase: “Solution structure of the nudix enzyme diadenosine tetraphosphate hydrolase from lupinus angustifolius…”. Solution nmr, 1 ligand (ATP), 1 pocket (best druggability 0.63). MolNFT…
- PDB
- 1JKN
- Type
- protein
- Length
- 165 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase
- EC
- 3.6.1.17
- UniProt
- O04841
- Ligands
- ATP
- Pockets
- 1 · best druggability 0.63
Structure
solution nmr · 1 distinct chain · 26% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Diadenosine 5',5'''-P1,P4-tetraphosphate hydrolase (EC 3.6.1.17) | protein | 165 | 26% helix, 28% strand | O04841 |
Ligands and binding sites
- ATP · Adenosine-5'-triphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 312 | 0.63 | 0.80 | 41 | ATP |
Compared structures
- 1JKN · Solution Structure of the Nudix Enzyme Diadenosine Tetraphosphate Hydrolase from Lupinus… · 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 O04841
- Elsewhere: RCSB PDB 1JKN · PDBe 1JKN · UniProt O04841
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