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Cryo-EM structure of the human pathogen mycoplasma pneumoniae P1

Analyse Cryo-EM structure of the human pathogen mycoplasma pneumoniae P1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BWM
Type
protein
Length
1,219 residues
Chains
1
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Adhesin P1
UniProt
P11311
Pockets
18 · best druggability 0.76

Structure

electron microscopy · 1 distinct chain · 19% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAdhesin P1protein121919% helix, 19% strandP11311

Pockets

18 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110090.760.7984empty
24580.690.8034empty
3530.650.9517empty
42800.640.8139empty
53650.640.7930empty

Compared structures

  • 7BWM · Cryo-EM structure of the human pathogen Mycoplasma pneumoniae P1 · the same entry in another collection · chain A against A, TM-score 1.00
  • P11311 · AlphaFold monomer V2.0 prediction for adhesin P1 (P11311) · a predicted model of the same protein · chain A against A, TM-score 0.99

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