MolNFT v1 · #107535 · protein
Structural plasticity of CID1 provides a basis for its RNA terminal uridylyl transferase activity
4UD5 · POLY(A) RNA polymerase protein CID1: “Structural plasticity of CID1 provides a basis for its RNA terminal uridylyl transferase activity”. X-ray diffraction, 5 pockets (best druggability 0.80). MolNFT v1 #107535 on GenesisL1: 3D…
- PDB
- 4UD5
- Type
- protein
- Length
- 680 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
- 5 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 44% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POLY(A) RNA polymerase protein CID1 (EC 2.7.7.-) | protein | 338 | 43% helix, 16% strand | O13833 |
| B | POLY(A) RNA polymerase protein CID1 (EC 2.7.7.-) | protein | 342 | 44% helix, 15% strand | O13833 |
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1091 | 0.80 | 0.81 | 89 | empty |
| 2 | 423 | 0.61 | 0.76 | 42 | empty |
| 3 | 440 | 0.59 | 0.75 | 50 | empty |
| 4 | 57 | 0.31 | 0.76 | 12 | empty |
| 5 | 50 | 0.25 | 0.73 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 597 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
- 4UD5 · Structural Plasticity of Cid1 Provides a Basis for its RNA Terminal Uridylyl 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 0.98
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 4UD5 · PDBe 4UD5 · UniProt O13833
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