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Ribosomal silencing factor during starvation or stationary phase (rsfs) from mycobacterium tuberculosis

Analyse Ribosomal silencing factor during starvation or stationary phase (rsfs) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4WCW
Type
protein
Length
462 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribosomal silencing factor rsfs
UniProt
O86327
Ligands
MG
Pockets
5 · best druggability 0.77

Structure

x-ray diffraction · 3 distinct chains · 36% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibosomal silencing factor rsfsprotein11635% helix, 28% strandO86327
BRibosomal silencing factor rsfsprotein11237% helix, 29% strandO86327
C, DRibosomal silencing factor rsfsprotein11735% helix, 27% strandO86327

Ligands and binding sites

  • MG · Magnesium ion · metal · 6 copies · chains A, B, C, D
  • MPD · (4S)-2-methyl-2,4-pentanediol · additive · 2 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15330.770.8452MPD
28430.750.7849empty
311300.750.7757empty
41660.540.8024MG
5520.260.7418empty

Interfaces

4 interfaces between chains.

  • A–B · 785 Ų buried · 28 hydrogen bonds · protein-protein
  • C–D · 736 Ų buried · 26 hydrogen bonds · protein-protein
  • A–C · 564 Ų buried · 10 hydrogen bonds · protein-protein
  • A–D · 396 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 4WCW · Ribosomal silencing factor during starvation or stationary phase (RsfS) from… · the same entry in another collection · chain A against A, TM-score 1.00

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