Research workbench
Crystal structure of apo human TUT1, form I
Analyse Crystal structure of apo human TUT1, form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WU1
- Type
- protein
- Length
- 977 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Speckle targeted PIP5K1A-regulated POLY(A) polymerase
- EC
- 2.7.7.19, 2.7.7.52
- UniProt
- Q9H6E5
- Ligands
- CL
- Pockets
- 12 · best druggability 0.69
Structure
x-ray diffraction · 2 distinct chains · 45% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Speckle targeted PIP5K1A-regulated POLY(A) polymerase (EC 2.7.7.19, 2.7.7.52) | protein | 493 | 46% helix, 15% strand | Q9H6E5 |
| B | Speckle targeted PIP5K1A-regulated POLY(A) polymerase (EC 2.7.7.19, 2.7.7.52) | protein | 484 | 45% helix, 15% strand | Q9H6E5 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 582 | 0.69 | 0.78 | 46 | empty |
| 2 | 524 | 0.68 | 0.79 | 43 | empty |
| 3 | 277 | 0.58 | 0.78 | 42 | empty |
| 4 | 264 | 0.58 | 0.78 | 42 | empty |
| 5 | 357 | 0.55 | 0.74 | 33 | empty |
Interfaces
1 interface between chains.
- A–B · 527 Ų buried · 2 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 Q9H6E5
- Elsewhere: RCSB PDB 5WU1 · PDBe 5WU1 · UniProt Q9H6E5
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