GL1X · GenesisL1 explorer

Research workbench

Reduced-form structure of E.COLI lon proteolytic domain

Analyse Reduced-form structure of E.COLI lon proteolytic domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3WU3
Type
protein
Length
1,102 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Lon protease
EC
3.4.21.53
UniProt
C9QQ79
Ligands
SO4
Pockets
16 · best druggability 0.58

Structure

x-ray diffraction · 4 distinct chains · 36% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ALon protease (EC 3.4.21.53)protein19038% helix, 30% strandC9QQ79
B, C, DLon protease (EC 3.4.21.53)protein18135% helix, 28% strandC9QQ79
ELon protease (EC 3.4.21.53)protein19034% helix, 27% strandC9QQ79
FLon protease (EC 3.4.21.53)protein17937% helix, 28% strandC9QQ79

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 5 copies · chains B, C, D, E, F

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12100.580.8029empty
21350.580.8425empty
31260.530.8122empty
41260.530.8126empty
51040.520.8323empty

Interfaces

6 interfaces between chains.

  • A–B · 1283 Ų buried · 25 hydrogen bonds · protein-protein
  • A–F · 795 Ų buried · 12 hydrogen bonds · protein-protein
  • B–C · 784 Ų buried · 13 hydrogen bonds · protein-protein
  • E–F · 763 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 760 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 3WU3 · Reduced-form structure of E.coli Lon Proteolytic domain · 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.