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Crystal structure of tdp-43 N-terminal domain at 2.1 a resolution

Analyse Crystal structure of tdp-43 N-terminal domain at 2.1 a resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MDI
Type
protein
Length
157 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tar DNA-binding protein 43
UniProt
K7EJM5
Pockets
2 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATar DNA-binding protein 43protein786% helix, 38% strandK7EJM5
BTar DNA-binding protein 43protein796% helix, 38% strandK7EJM5

Ligands and binding sites

  • ACT · Acetate ion · additive · chains B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1600.350.7820empty
2940.320.7320empty

Interfaces

1 interface between chains.

  • A–B · 696 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (nonstandard).

Compared structures

  • 5MDI · Crystal structure of TDP-43 N-terminal domain at 2.1 A resolution · the same entry in another collection · chain A against A, TM-score 1.00

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