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Structure of the spoiiq-spoiiiah pore forming complex.

Analyse Structure of the spoiiq-spoiiiah pore forming complex. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TUF
Type
protein
Length
273 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Stage III sporulation protein ah; Stage II sporulation protein Q
UniProt
P49785, P71044
Pockets
2 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AStage III sporulation protein ahprotein11558% helix, 16% strandP49785
BStage II sporulation protein Qprotein15812% helix, 44% strandP71044

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11320.440.7726empty
2980.370.7518empty

Interfaces

1 interface between chains.

  • A–B · 835 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 3TUF · Structure of the SpoIIQ-SpoIIIAH pore forming complex. · the same entry in another collection · chain A against A, TM-score 1.00
  • P71044 · AlphaFold monomer V2.0 prediction for stage II sporulation protein Q (P71044) · a predicted model of the same protein · chain B against A, TM-score 0.99
  • P49785 · AlphaFold monomer V2.0 prediction for stage III sporulation protein ah (P49785) · a predicted model of the same protein · chain A against A, TM-score 0.90

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