GL1X · GenesisL1 explorer

Research workbench

Circular permutant of ribosomal protein S6, swap helix 2, L75A mutant

Analyse Circular permutant of ribosomal protein S6, swap helix 2, L75A mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6I6O
Type
protein
Length
410 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
30S ribosomal protein S6,30S ribosomal protein S6
UniProt
Q5SLP8
Pockets
5 · best druggability 0.86

Structure

x-ray diffraction · 4 distinct chains · 31% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A30S ribosomal protein S6,30S ribosomal protein S6protein9929% helix, 45% strandQ5SLP8
B30S ribosomal protein S6,30S ribosomal protein S6protein10633% helix, 42% strandQ5SLP8
C30S ribosomal protein S6,30S ribosomal protein S6protein10535% helix, 43% strandQ5SLP8
D30S ribosomal protein S6,30S ribosomal protein S6protein10026% helix, 45% strandQ5SLP8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111140.860.87112empty
21550.800.9625empty
31970.720.8832empty
41190.440.7725empty
5920.390.7622empty

Interfaces

5 interfaces between chains.

  • A–C · 1688 Ų buried · 24 hydrogen bonds · protein-protein
  • B–D · 1546 Ų buried · 23 hydrogen bonds · protein-protein
  • A–D · 888 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 282 Ų buried · 3 hydrogen bonds · protein-protein
  • A–B · 175 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 6I6O · Circular permutant of ribosomal protein S6, swap helix 2, L75A mutant · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.