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Cdtb double heptamer short form modeled from cryo-EM MAP reconstructed using C1 symmetry

Analyse Cdtb double heptamer short form modeled from cryo-EM MAP reconstructed using C1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6O2O
Type
protein
Length
9,218 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ADP-ribosyltransferase binding component
UniProt
A8DS70
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 3 distinct chains · 9% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, D, F, H, J, LADP-ribosyltransferase binding componentprotein6598% helix, 37% strandA8DS70
C, E, G, I, K, MADP-ribosyltransferase binding componentprotein6589% helix, 29% strandA8DS70
ZADP-ribosyltransferase binding componentprotein6579% helix, 28% strandA8DS70

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111020.880.90146empty
29970.870.88114empty
38760.840.8684empty
48930.840.86102empty
59880.840.85106empty

Interfaces

35 interfaces between chains.

  • J–L · 4136 Ų buried · 77 hydrogen bonds · protein-protein
  • A–B · 4104 Ų buried · 75 hydrogen bonds · protein-protein
  • A–L · 4103 Ų buried · 65 hydrogen bonds · protein-protein
  • H–J · 3991 Ų buried · 76 hydrogen bonds · protein-protein
  • F–H · 3983 Ų buried · 74 hydrogen bonds · protein-protein

Compared structures

  • 6O2O · CDTb Double Heptamer Short Form Modeled from Cryo-EM Map Reconstructed using C1 Symmetry · the same entry in another collection · chain A against A, TM-score 1.00

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