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Crystal structure of transcriptional activator tena from bacillus subtilis

Analyse Crystal structure of transcriptional activator tena from bacillus subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TYH
Type
protein
Length
884 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transcriptional activator tena
UniProt
P25052
Pockets
11 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 78% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, D, ETranscriptional activator tenaprotein22178% helix, 0% strandP25052

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18160.760.8078empty
2780.750.9716empty
311290.740.7792empty
43320.740.8544empty
52250.730.8839empty

Interfaces

6 interfaces between chains.

  • A–D · 1098 Ų buried · 19 hydrogen bonds · protein-protein
  • B–E · 1094 Ų buried · 19 hydrogen bonds · protein-protein
  • B–D · 952 Ų buried · 6 hydrogen bonds · protein-protein
  • A–E · 945 Ų buried · 4 hydrogen bonds · protein-protein
  • A–B · 156 Ų buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 20 modified (engineered).

Compared structures

  • 1TYH · Crystal Structure of Transcriptional Activator tenA from Bacillus subtilis · the same entry in another collection · chain A against A, TM-score 1.00
  • P25052 · AlphaFold monomer V2.0 prediction for aminopyrimidine aminohydrolase (P25052) · a predicted model of the same protein · chain A against A, TM-score 1.00

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