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Structural characterization of the late competence protein comfb from bacillus subtilis.

Analyse Structural characterization of the late competence protein comfb from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4WAI
Type
protein
Length
359 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Comf operon protein 2
UniProt
P39146
Ligands
ZN
Pockets
4 · best druggability 0.48

Structure

x-ray diffraction · 3 distinct chains · 60% helix, 4% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, CComf operon protein 2protein9160% helix, 4% strandP39146
BComf operon protein 2protein8956% helix, 4% strandP39146
DComf operon protein 2protein8863% helix, 5% strandP39146

Ligands and binding sites

  • ZN · Zinc ion · metal · 4 copies · chains A, C, B, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11730.480.7632empty
21640.480.7721empty
3510.330.7813empty
4550.280.7416empty

Interfaces

4 interfaces between chains.

  • C–D · 838 Ų buried · 14 hydrogen bonds · protein-protein
  • A–B · 811 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 688 Ų buried · 3 hydrogen bonds · protein-protein
  • C–B · 103 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 4WAI · Structural characterization of the late competence protein ComFB from Bacillus subtilis. · the same entry in another collection · chain C against C, TM-score 1.00
  • P39146 · AlphaFold monomer V2.0 prediction for comf operon protein 2 (P39146) · a predicted model of the same protein · chain D against A, TM-score 0.95

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