Research workbench
Solution structure of a human cancer-related nucleoside triphosphatase
Analyse Solution structure of a human cancer-related nucleoside triphosphatase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I3B
- Type
- protein
- Length
- 189 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human cancer-related NTPase
- EC
- 3.6.1.15
- UniProt
- Q5TDE9
- Pockets
- 3 · best druggability 0.62
Structure
solution nmr · 1 distinct chain · 25% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human cancer-related NTPase (EC 3.6.1.15) | protein | 189 | 25% helix, 21% strand | Q5TDE9 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 273 | 0.62 | 0.80 | 30 | empty |
| 2 | 59 | 0.40 | 0.81 | 18 | empty |
| 3 | 80 | 0.39 | 0.78 | 18 | empty |
Compared structures
- 2I3B · Solution Structure of a Human Cancer-Related Nucleoside Triphosphatase · 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 Q5TDE9
- Elsewhere: RCSB PDB 2I3B · PDBe 2I3B · UniProt Q5TDE9
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