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Crystal structure from a domain (Thr161-F265) from fructose-specific iiabc component (Pts system) from Borrelia burgdorferi

Analyse Crystal structure from a domain (Thr161-F265) from fructose-specific iiabc… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5DLE
Type
protein
Length
416 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.55
Source
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Molecule
Pts system, fructose-specific iiabc component
UniProt
O51369
Ligands
CL
Pockets
3 · best druggability 0.55

Structure

x-ray diffraction · resolution 1.55 · 1 distinct chain · 38% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DPts system, fructose-specific iiabc componentprotein10438% helix, 27% strandO51369

Ligands and binding sites

  • CL · Chloride ion · ion · chains A, B
  • IMD · Imidazole · additive · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11520.550.8129empty
21220.440.7728empty
3710.330.7616empty

Interfaces

5 interfaces between chains.

  • B–C · 555 Ų buried · 6 hydrogen bonds · protein-protein
  • A–D · 544 Ų buried · 6 hydrogen bonds · protein-protein
  • A–C · 372 Ų buried · 3 hydrogen bonds · protein-protein
  • B–D · 370 Ų buried · 2 hydrogen bonds · protein-protein
  • A–B · 131 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 5DLE · Crystal structure from a domain (THR161-F265) from fructose-specific iiabc component (pts… · the same entry in another collection · chain A against A, TM-score 1.00

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