GL1X · GenesisL1 explorer

Research workbench

Outer surface protein B of B. burgdorferi: crystal structure of the C-terminal fragment

Analyse Outer surface protein B of B. burgdorferi: crystal structure of the C-terminal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1P4P
Type
protein
Length
140 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Outer surface protein B
UniProt
P17739
Pockets
1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 9% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AOuter surface protein Bprotein1409% helix, 56% strandP17739

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1820.370.7618empty

Compared structures

  • 1P4P · Outer Surface Protein B of B. burgdorferi: crystal structure of the C-terminal fragment · the same entry in another collection · chain A against A, TM-score 1.00
  • P17739 · AlphaFold monomer V2.0 prediction for outer surface protein B (P17739) · a predicted model of the same protein · chain A against A, TM-score 0.97

Analyse

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