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Crystal structure of an outer surface protein BBA66 from borrelia burgdorferi

Analyse Crystal structure of an outer surface protein BBA66 from borrelia burgdorferi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2YN7
Type
protein
Length
428 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Outer surface protein
UniProt
O50955
Pockets
3 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 75% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BOuter surface proteinprotein21475% helix, 1% strandO50955

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12260.550.7831empty
22680.550.7738empty
31130.380.7527empty

Interfaces

1 interface between chains.

  • A–B · 827 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 2YN7 · Crystal structure of an outer surface protein BBA66 from Borrelia burgdorferi · the same entry in another collection · chain A against A, TM-score 1.00

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