MolNFT v1 · #90078 · protein
Structural basis for the activity of a cytoplasmic RNA terminal U- transferase
4E8F · POLY(A) RNA polymerase protein CID1: “Structural basis for the activity of a cytoplasmic RNA terminal U- transferase”. X-ray diffraction, 10 pockets (best druggability 0.75). MolNFT v1 #90078 on GenesisL1: 3D structure, binding…
- PDB
- 4E8F
- Type
- protein
- Length
- 646 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- POLY(A) RNA polymerase protein CID1
- EC
- 2.7.7.-
- UniProt
- O13833
- Pockets
- 10 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 41% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POLY(A) RNA polymerase protein CID1 (EC 2.7.7.-) | protein | 327 | 43% helix, 14% strand | O13833 |
| B | POLY(A) RNA polymerase protein CID1 (EC 2.7.7.-) | protein | 319 | 39% helix, 14% strand | O13833 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 540 | 0.75 | 0.83 | 84 | empty |
| 2 | 637 | 0.66 | 0.76 | 55 | ACT |
| 3 | 225 | 0.66 | 0.84 | 30 | empty |
| 4 | 378 | 0.60 | 0.76 | 42 | GOL |
| 5 | 125 | 0.49 | 0.80 | 26 | ACT |
Interfaces
1 interface between chains.
- A–B · 1006 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 4E8F · Structural Basis for the Activity of a Cytoplasmic RNA Terminal U-transferase · the same entry in another collection · chain A against A, TM-score 1.00
- O13833 · AlphaFold monomer V2.0 prediction for terminal uridylyltransferase CID1 (O13833) · 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 O13833
- Elsewhere: RCSB PDB 4E8F · PDBe 4E8F · UniProt O13833
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