Research workbench
Solution structure of the nudix enzyme diadenosine tetraphosphate hydrolase from lupinus angustifolius L.
Analyse Solution structure of the nudix enzyme diadenosine tetraphosphate hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F3Y
- 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
- Pockets
- 1 · best druggability 0.39
Structure
solution nmr · 1 distinct chain · 30% 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 | 30% helix, 28% strand | O04841 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 93 | 0.39 | 0.76 | 16 | empty |
Compared structures
- 1F3Y · 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 1F3Y · PDBe 1F3Y · UniProt O04841
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