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Crystal structure of bordetella pertussis bvgs VFT2 domain (double mutant F375E/Q461E)

Analyse Crystal structure of bordetella pertussis bvgs VFT2 domain (double mutant… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3MPL
Type: protein
Length: 233 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Virulence sensor protein bvgs
UniProt: P16575
Pockets: 1 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 31% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Virulence sensor protein bvgs	protein	233	36% helix, 31% strand	P16575

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	170	0.78	0.94	30	EDO

Compared structures

3MPL · Crystal Structure of Bordetella pertussis BvgS VFT2 domain (Double Mutant F375E/Q461E) · the same entry in another collection · chain A against A, TM-score 1.00
P16575 · AlphaFold monomer V2.0 prediction for virulence sensor protein bvgs (P16575) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P16575
Elsewhere: RCSB PDB 3MPL · PDBe 3MPL · UniProt P16575

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