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T. maritima flig C-terminal domain

Analyse T. maritima flig C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1QC7
Type
protein
Length
190 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (flig)
UniProt
Q9WY63
Pockets
2 · best druggability 0.62

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (flig)protein10163% helix, 2% strandQ9WY63
BProtein (flig)protein8973% helix, 0% strandQ9WY63

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12990.620.8024empty
22900.560.7635empty

Interfaces

1 interface between chains.

  • A–B · 519 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 1QC7 · T. maritima flig C-terminal domain · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9WY63 · AlphaFold monomer V2.0 prediction for flagellar motor switch protein flig (Q9WY63) · a predicted model of the same protein · chain B against A, TM-score 0.95

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