Research workbench
Crystal structures of the CID1 poly (U) polymerase reveal the mechanism for UTP selectivity - mg 3'-datp bound
Analyse Crystal structures of the CID1 poly (U) polymerase reveal the mechanism for UTP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FHY
- Type
- protein
- Length
- 318 residues
- Chains
- 1
- 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
- Ligands
- 3AT, MG
- Pockets
- 1 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | POLY(A) RNA polymerase protein CID1 (EC 2.7.7.-) | protein | 318 | 46% helix, 14% strand | O13833 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 727 | 0.68 | 0.76 | 54 | 3AT, MG |
Compared structures
- 4FHY · Crystal structures of the Cid1 poly (U) polymerase reveal the mechanism for UTP… · 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 4FHY · PDBe 4FHY · UniProt O13833
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.