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Vibrio parahaemolyticus VTRA/VTRC complex

Analyse Vibrio parahaemolyticus VTRA/VTRC complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5KEV
Type
protein
Length
216 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Vtra protein; Vtrc protein
UniProt
Q87GI4, Q87GI3
Ligands
SO4
Pockets
3 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 51% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AVtra proteinprotein9033% helix, 31% strandQ87GI4
BVtrc proteinprotein1266% helix, 66% strandQ87GI3

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13270.790.8852empty
2590.410.8118empty
3790.300.7322empty

Interfaces

1 interface between chains.

  • A–B · 1227 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 5KEV · Vibrio parahaemolyticus VtrA/VtrC complex · the same entry in another collection · chain A against A, TM-score 1.00

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