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Crystal structure of self-complemented myfa, the major subunit of myf fimbriae from yersinia enterocolitica

Analyse Crystal structure of self-complemented myfa, the major subunit of myf fimbriae… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5LO7
Type
protein
Length
251 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fimbrial protein MYFA,FIMBRIAL protein myfa
UniProt
P33406
Pockets
1 · best druggability 0.46

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 57% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFimbrial protein MYFA,FIMBRIAL protein myfaprotein1252% helix, 57% strandP33406
BFimbrial protein MYFA,FIMBRIAL protein myfaprotein1262% helix, 58% strandP33406

Ligands and binding sites

  • PG0 · 2-(2-methoxyethoxy)ethanol · additive · chains B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1690.460.8320empty

Interfaces

1 interface between chains.

  • A–B · 359 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 5LO7 · Crystal structure of self-complemented MyfA, the major subunit of Myf fimbriae from… · the same entry in another collection · chain A against A, TM-score 1.00
  • P33406 · AlphaFold monomer V2.0 prediction for fimbrial protein myfa (P33406) · a predicted model of the same protein · chain A against A, TM-score 0.86

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