Research workbench
Structure of human TULP1 in complex with IP3
Analyse Structure of human TULP1 in complex with IP3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C5N
- Type
- protein
- Length
- 454 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Tubby-related protein 1
- UniProt
- O00294
- Ligands
- I3P
- Pockets
- 8 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 11% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Tubby-related protein 1 | protein | 231 | 11% helix, 38% strand | O00294 |
| B | Tubby-related protein 1 | protein | 223 | 11% helix, 39% strand | O00294 |
Ligands and binding sites
- I3P · D-myo-inositol-1,4,5-triphosphate · ligand · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1058 | 0.74 | 0.77 | 80 | I3P |
| 2 | 98 | 0.48 | 0.81 | 20 | empty |
| 3 | 90 | 0.45 | 0.80 | 24 | empty |
| 4 | 63 | 0.39 | 0.80 | 18 | empty |
| 5 | 66 | 0.32 | 0.76 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 489 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
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 O00294
- Elsewhere: RCSB PDB 3C5N · PDBe 3C5N · UniProt O00294
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