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The crystal structure of tellurite resistance protein from escherichia COLI O157:H7 str. sakai

Analyse The crystal structure of tellurite resistance protein from escherichia COLI… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4DQ0
Type
protein
Length
784 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tellurite resistance protein
UniProt
Q8X9V6
Pockets
9 · best druggability 0.86

Structure

x-ray diffraction · 3 distinct chains · 28% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATellurite resistance proteinprotein19529% helix, 30% strandQ8X9V6
B, CTellurite resistance proteinprotein19827% helix, 30% strandQ8X9V6
DTellurite resistance proteinprotein19328% helix, 33% strandQ8X9V6

Ligands and binding sites

  • NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 5 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15050.860.9273NHE
25950.850.9071empty
35920.850.9079NHE
44110.600.7646empty
52010.580.8032empty

Interfaces

6 interfaces between chains.

  • A–B · 1457 Ų buried · 24 hydrogen bonds · protein-protein
  • C–D · 1400 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 277 Ų buried · 4 hydrogen bonds · protein-protein
  • A–D · 213 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 211 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 4DQ0 · The crystal structure of tellurite resistance protein from Escherichia coli O157:H7 str.… · the same entry in another collection · chain A against A, TM-score 1.00

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