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Cdtb double heptamer long form modeled from cryo-EM MAP reconstructed using C7 symmetry

Analyse Cdtb double heptamer long 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: 6O2M
Type: protein
Length: 8,652 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 0.79

Structure

electron microscopy · 1 distinct chain · 9% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D, E, F, G, T, U, V, W, X, Y, Z	ADP-ribosyltransferase binding component	protein	618	9% helix, 35% strand	A8DS70

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	110	0.79	0.98	27	empty
2	1071	0.79	0.81	136	empty
3	103	0.79	0.98	27	empty
4	106	0.78	0.98	28	empty
5	801	0.78	0.82	103	empty

Interfaces

35 interfaces between chains.

A–B · 3081 Å² buried · 50 hydrogen bonds · protein-protein
T–U · 2959 Å² buried · 34 hydrogen bonds · protein-protein
V–W · 2919 Å² buried · 24 hydrogen bonds · protein-protein
Y–Z · 2796 Å² buried · 35 hydrogen bonds · protein-protein
T–Z · 2789 Å² buried · 43 hydrogen bonds · protein-protein

Compared structures

6O2M · CDTb Double Heptamer Long 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

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt A8DS70
Elsewhere: RCSB PDB 6O2M · PDBe 6O2M · UniProt A8DS70

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