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Crystal structure of BSE31 (BSPA14S_RS05060 gene product) from Lyme disease agent Borrelia (Borreliella) spielmanii

Analyse Crystal structure of BSE31 (BSPA14S_RS05060 gene product) from Lyme disease… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6FZZ
Type: protein
Length: 199 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.05
Source: Borreliella spielmanii A14S
Molecule: Virulent strain associated lipoprotein
UniProt: C0RBM0
Pockets: 2 · best druggability 0.46

Structure

x-ray diffraction · resolution 2.05 · 1 distinct chain · 80% helix, 1% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Virulent strain associated lipoprotein	protein	199	80% helix, 1% strand	C0RBM0

Ligands and binding sites

PG4 · Tetraethylene glycol · additive · 4 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	106	0.46	0.79	20	PG4
2	65	0.41	0.80	12	empty

Compared structures

6FZZ · Crystal structure of BSE31 (BSPA14S_RS05060 gene product) from lyme disease agent… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt C0RBM0
Elsewhere: RCSB PDB 6FZZ · PDBe 6FZZ · UniProt C0RBM0

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