GL1X · GenesisL1 explorer

MolNFT v1 · #87411 · protein

Extended interface between PCF11P and CLP1P and structural basis for ATP loss in GLY135ARG point mutant

4C0H · MRNA cleavage and polyadenylation factor CLP1: “Extended interface between PCF11P and CLP1P and structural basis for ATP loss in GLY135ARG point mutant”. X-ray diffraction, 9 pockets (best druggability 0.76). MolNFT v1 #87411 on…

PDB
4C0H
Type
protein
Length
910 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
MRNA cleavage and polyadenylation factor CLP1; PCF11P
UniProt
Q08685, N1P6M1
Pockets
9 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 29% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMRNA cleavage and polyadenylation factor CLP1protein42229% helix, 30% strandQ08685
BMRNA cleavage and polyadenylation factor CLP1protein42730% helix, 30% strandQ08685
CPCF11Pprotein2829% helix, 4% strandN1P6M1
DPCF11Pprotein3324% helix, 9% strandN1P6M1

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15240.760.8443empty
21410.650.8728empty
32550.620.8142empty
41560.540.8122empty
51690.530.7924empty

Interfaces

3 interfaces between chains.

  • B–D · 2035 Ų buried · 34 hydrogen bonds · protein-protein
  • A–C · 1885 Ų buried · 33 hydrogen bonds · protein-protein
  • A–B · 955 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 4C0H · Extended interface between Pcf11p and Clp1p and structural basis for ATP loss in… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q08685 · AlphaFold monomer V2.0 prediction for mRNA cleavage and polyadenylation factor CLP1… · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

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