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Crystal structure of E.COLI maca

Analyse Crystal structure of E.COLI maca in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3FPP
Type
protein
Length
533 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Macrolide-specific efflux protein maca
UniProt
P75830
Pockets
5 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 29% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMacrolide-specific efflux protein macaprotein26628% helix, 27% strandP75830
BMacrolide-specific efflux protein macaprotein26730% helix, 30% strandP75830

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11280.560.8319empty
23300.540.7432empty
31850.520.7829empty
4910.350.7523empty
5680.290.7320empty

Interfaces

1 interface between chains.

  • A–B · 2011 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 3FPP · Crystal structure of E.coli MacA · the same entry in another collection · chain A against A, TM-score 1.00
  • P75830 · AlphaFold monomer V2.0 prediction for macrolide export protein maca (P75830) · a predicted model of the same protein · chain A against A, TM-score 0.96

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