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MolNFT v1 · #107534 · protein

Structural plasticity of CID1 provides a basis for its RNA terminal uridylyl transferase activity

4UD4 · POLY(A) RNA polymerase protein CID1: “Structural plasticity of CID1 provides a basis for its RNA terminal uridylyl transferase activity”. X-ray diffraction, 6 pockets (best druggability 0.78). MolNFT v1 #107534 on GenesisL1: 3D…

PDB
4UD4
Type
protein
Length
641 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
6 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 46% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APOLY(A) RNA polymerase protein CID1 (EC 2.7.7.-)protein32446% helix, 13% strandO13833
BPOLY(A) RNA polymerase protein CID1 (EC 2.7.7.-)protein31746% helix, 13% strandO13833

Ligands and binding sites

  • GOL · Glycerol · additive · 2 copies · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13270.780.8948empty
25610.630.7562empty
32570.540.7638empty
4600.420.8111empty
5820.310.7317empty

Interfaces

1 interface between chains.

  • A–B · 403 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 4UD4 · 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 0.99

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