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Crystal structure of BBA68 or bbcrasp-1 from borrelia burgdorferi strain B31

Analyse Crystal structure of BBA68 or bbcrasp-1 from borrelia burgdorferi strain B31 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5A2U
Type
protein
Length
355 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Complement regulator acquiring protein 1
UniProt
Q66ZA0
Pockets
3 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 76% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AComplement regulator acquiring protein 1protein18175% helix, 1% strandQ66ZA0
BComplement regulator acquiring protein 1protein17477% helix, 0% strandQ66ZA0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14480.580.7437empty
2690.420.8017empty
3790.360.7513empty

Interfaces

1 interface between chains.

  • A–B · 79 Ų buried · 3 hydrogen bonds · protein-protein

Compared structures

  • 5A2U · Crystal structure of BBA68 or BbCRASP-1 from Borrelia burgdorferi strain B31 · the same entry in another collection · chain A against A, TM-score 1.00

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