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Ftsz dimer, empty (M. jannaschii)

Analyse Ftsz dimer, empty (M. jannaschii) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1W59
Type
protein
Length
693 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cell division protein ftsz homolog 1
UniProt
Q57816
Ligands
SO4
Pockets
8 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 45% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACell division protein ftsz homolog 1protein35047% helix, 23% strandQ57816
BCell division protein ftsz homolog 1protein34343% helix, 24% strandQ57816

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17240.810.8577SO4
21260.600.8533empty
31590.510.7931SO4
41500.490.7831empty
5630.400.8014empty

Interfaces

1 interface between chains.

  • A–B · 1235 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 1W59 · FtsZ dimer, empty (M. jannaschii) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q57816 · AlphaFold monomer V2.0 prediction for cell division protein ftsz 1 (Q57816) · a predicted model of the same protein · chain B against A, TM-score 0.96

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