GL1X · GenesisL1 explorer

Research workbench

CDTb Double Heptamer Short Form Modeled from Cryo-EM Map Reconstructed using C7 Symmetry

Analyse CDTb Double Heptamer Short Form Modeled from Cryo-EM Map Reconstructed using C7… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6O2N
Type
protein
Length
9,218 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.7
Source
Clostridioides difficile
Molecule
ADP-ribosyltransferase binding component
UniProt
A8DS70
Pockets
20 · best druggability 0.84

Structure

electron microscopy · resolution 3.7 · 3 distinct chains · 9% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, D, F, H, J, LADP-ribosyltransferase binding componentprotein65910% helix, 39% strandA8DS70
C, E, G, I, K, MADP-ribosyltransferase binding componentprotein6589% helix, 29% strandA8DS70
ZADP-ribosyltransferase binding componentprotein6578% helix, 30% strandA8DS70

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18650.840.8696empty
28110.840.8790empty
310310.840.85113empty
47820.830.8683empty
57770.830.8680empty

Interfaces

35 interfaces between chains.

  • J–L · 4143 Ų buried · 50 hydrogen bonds · protein-protein
  • B–D · 4139 Ų buried · 46 hydrogen bonds · protein-protein
  • F–H · 4131 Ų buried · 59 hydrogen bonds · protein-protein
  • D–F · 4120 Ų buried · 46 hydrogen bonds · protein-protein
  • A–B · 4118 Ų buried · 49 hydrogen bonds · protein-protein

Compared structures

  • 6O2N · Cdtb double heptamer short form modeled from cryo-EM MAP reconstructed using C7 symmetry · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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