Research workbench

Crystal structures of the CID1 poly (U) polymerase reveal the mechanism for UTP selectivity

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: 4FH3
Type: protein
Length: 323 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
Pockets: 2 · best druggability 0.67

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	323	46% helix, 14% strand	O13833

Pockets

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	688	0.67	0.75	53	empty
2	65	0.32	0.75	13	empty

Compared structures

4FH3 · 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 4FH3 · PDBe 4FH3 · UniProt O13833

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.