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MolNFT v1 · #188626 · protein

TMEM106B(120-254) T185S protofilament from frontotemporal lobar degeneration with tdp-43 pathology (ftld-tdp) type a (all cases combined).

7U18 · TMEM106B protein: “TMEM106B(120-254) T185S protofilament from frontotemporal lobar degeneration with tdp-43 pathology (ftld-tdp)…”. Electron microscopy, 1 ligand (NAG), 4 pockets (best druggability 0.53). MolNFT v1 #188626 on…

PDB
7U18
Type
protein
Length
405 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TMEM106B protein
UniProt
Q8N353
Ligands
NAG
Pockets
4 · best druggability 0.53

Structure

electron microscopy · 1 distinct chain · 0% helix, 76% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CTMEM106B proteinprotein1350% helix, 76% strandQ8N353

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 12 copies · chains A, B, C

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12400.530.7627empty
21130.530.8222empty
31340.510.7920empty
42130.460.7436empty

Interfaces

3 interfaces between chains.

  • B–C · 5973 Ų buried · 191 hydrogen bonds · protein-protein
  • A–B · 5971 Ų buried · 193 hydrogen bonds · protein-protein
  • A–C · 82 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 12 glycan, 3 disulfide (N-glycosylation, disulfide).

Compared structures

  • 7U18 · TMEM106B(120-254) T185S protofilament from frontotemporal lobar degeneration with TDP-43… · the same entry in another collection · chain A against A, TM-score 1.00

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