GL1X · GenesisL1 explorer

Research workbench

Periplasmic domain of vibrio parahaemolyticus cpxa

Analyse Periplasmic domain of vibrio parahaemolyticus cpxa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3V67
Type
protein
Length
263 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sensor protein cpxa
EC
2.7.13.3
UniProt
Q87KW6
Pockets
2 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASensor protein cpxa (EC 2.7.13.3)protein13230% helix, 27% strandQ87KW6
BSensor protein cpxa (EC 2.7.13.3)protein13131% helix, 27% strandQ87KW6

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14510.780.8656empty
2680.640.9219empty

Interfaces

1 interface between chains.

  • A–B · 1322 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 3V67 · Periplasmic domain of Vibrio parahaemolyticus CpxA · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.