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Structural and functional analysis of the E. COLI nusb-S10 transcription antitermination complex.

Analyse Structural and functional analysis of the E. COLI nusb-S10 transcription… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3D3C
Type
protein
Length
673 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N utilization substance protein B; 30S ribosomal protein S10
UniProt
P0A780, P0A7R5
Pockets
7 · best druggability 0.70

Structure

x-ray diffraction · 3 distinct chains · 50% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CN utilization substance protein Bprotein13873% helix, 0% strandP0A780
J30S ribosomal protein S10protein8531% helix, 41% strandP0A7R5
K, L30S ribosomal protein S10protein8733% helix, 40% strandP0A7R5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16620.700.7853empty
2720.580.8917empty
3630.570.8921empty
41390.460.7614empty
5640.450.8216empty

Interfaces

9 interfaces between chains.

  • C–L · 960 Ų buried · 11 hydrogen bonds · protein-protein
  • B–K · 955 Ų buried · 14 hydrogen bonds · protein-protein
  • A–J · 890 Ų buried · 15 hydrogen bonds · protein-protein
  • A–K · 397 Ų buried · 5 hydrogen bonds · protein-protein
  • B–C · 357 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 3D3C · Structural and functional analysis of the E. coli NusB-S10 transcription antitermination… · the same entry in another collection · chain B against B, TM-score 1.00
  • P0A780 · AlphaFold monomer V2.0 prediction for transcription antitermination protein nusb (P0A780) · a predicted model of the same protein · chain A against A, TM-score 0.96

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