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Periplasmic domain of epsm from vibrio cholerae

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

PDB
1UV7
Type
protein
Length
150 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
General secretion pathway protein M
UniProt
P41851
Pockets
1 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 34% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGeneral secretion pathway protein Mprotein7634% helix, 41% strandP41851
BGeneral secretion pathway protein Mprotein7434% helix, 43% strandP41851

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11830.560.7927empty

Interfaces

1 interface between chains.

  • A–B · 505 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

  • 1UV7 · periplasmic domain of EpsM from Vibrio cholerae · the same entry in another collection · chain A against A, TM-score 1.00
  • P41851 · AlphaFold monomer V2.0 prediction for type II secretion system protein M (P41851) · a predicted model of the same protein · chain B against A, TM-score 0.99

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