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Crystal structure of SPO0M, sporulation control protein, from bacillus subtilis.

Analyse Crystal structure of SPO0M, sporulation control protein, from bacillus subtilis. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5CL2
Type
protein
Length
491 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sporulation-control protein SPO0M
UniProt
P71088
Ligands
NA
Pockets
4 · best druggability 0.84

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 49% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASporulation-control protein SPO0Mprotein24617% helix, 49% strandP71088
BSporulation-control protein SPO0Mprotein24517% helix, 49% strandP71088

Ligands and binding sites

  • NA · Sodium ion · metal · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12420.840.9655empty
21610.400.7332empty
31050.340.7323empty
4540.260.7415empty

Interfaces

1 interface between chains.

  • A–B · 893 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 5CL2 · Crystal structure of Spo0M, sporulation control protein, from Bacillus subtilis. · the same entry in another collection · chain A against A, TM-score 1.00
  • P71088 · AlphaFold monomer V2.0 prediction for sporulation-control protein SPO0M (P71088) · a predicted model of the same protein · chain B against A, TM-score 1.00

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