Research workbench
Crystal structure of human TUT1 bound with bautp, form I
Analyse Crystal structure of human TUT1 bound with bautp, form I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5WU2
- Type
- protein
- Length
- 968 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
- UTP, BA, CL
- Pockets
- 12 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Speckle targeted PIP5K1A-regulated POLY(A) polymerase (EC 2.7.7.19, 2.7.7.52) | protein | 484 | 46% helix, 15% strand | Q9H6E5 |
Ligands and binding sites
- UTP · Uridine 5'-triphosphate · ligand · 2 copies · chains A, B
- BA · Barium ion · metal · 2 copies · chains A, B
- 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 | 592 | 0.69 | 0.78 | 43 | UTP, BA |
| 2 | 509 | 0.69 | 0.79 | 46 | UTP, BA |
| 3 | 287 | 0.59 | 0.78 | 40 | empty |
| 4 | 276 | 0.59 | 0.78 | 44 | empty |
| 5 | 338 | 0.54 | 0.74 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 493 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5WU2 · Crystal structure of human Tut1 bound with BaUTP, form I · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H6E5 · AlphaFold monomer V2.0 prediction for speckle targeted PIP5K1A-regulated POLY(A)… · a predicted model of the same protein · chain A against A, TM-score 0.99
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 5WU2 · PDBe 5WU2 · UniProt Q9H6E5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.