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Crystal structure of mycobacterial ftsx extracellular domain, bromide derivative

Analyse Crystal structure of mycobacterial ftsx extracellular domain, bromide derivative in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4N8O
Type
protein
Length
198 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cell division protein ftsx
UniProt
P9WG19
Ligands
K, BR
Pockets
1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BCell division protein ftsxprotein9939% helix, 22% strandP9WG19

Ligands and binding sites

  • K · Potassium ion · metal · 4 copies · chains A, B
  • BR · Bromide ion · ion · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1600.510.8722empty

Interfaces

1 interface between chains.

  • A–B · 519 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

  • 4N8O · Crystal structure of Mycobacterial FtsX extracellular domain, bromide derivative · the same entry in another collection · chain A against A, TM-score 1.00
  • P9WG19 · AlphaFold monomer V2.0 prediction for cell division protein ftsx (P9WG19) · a predicted model of the same protein · chain A against A, TM-score 0.97

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