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Sega-long, conformation of tdp-43 low complexity domain segment a long

Analyse Sega-long, conformation of tdp-43 low complexity domain segment a long in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6N3A
Type
protein
Length
600 residues
Chains
20
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tar DNA-binding protein 43; Sega long small
UniProt
Q13148
Pockets
2 · best druggability 0.37

Structure

electron microscopy · 2 distinct chains · 0% helix, 60% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, JTar DNA-binding protein 43protein500% helix, 62% strandQ13148
K, L, M, N, O, P, Q, R, S, TSega long smallprotein100% helix, 50% strand—

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1980.370.7521empty
2800.370.7719empty

Interfaces

59 interfaces between chains.

  • A–F · 1968 Ų buried · 74 hydrogen bonds · protein-protein
  • F–I · 1966 Ų buried · 74 hydrogen bonds · protein-protein
  • B–E · 1964 Ų buried · 74 hydrogen bonds · protein-protein
  • C–H · 1964 Ų buried · 74 hydrogen bonds · protein-protein
  • D–G · 1963 Ų buried · 73 hydrogen bonds · protein-protein

Compared structures

  • 6N3A · SegA-long, conformation of TDP-43 low complexity domain segment A long · the same entry in another collection · chain T against T, TM-score 1.00

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