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Tryptophan repressor trpr from E.COLI with 5-methyltryptamine

Analyse Tryptophan repressor trpr from E.COLI with 5-methyltryptamine in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6F7G
Type
protein
Length
201 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
TRP operon repressor
UniProt
P0A881
Ligands
CVW
Pockets
2 · best druggability 0.49

Structure

x-ray diffraction · 2 distinct chains · 81% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATRP operon repressorprotein10380% helix, 0% strandP0A881
CTRP operon repressorprotein9882% helix, 0% strandP0A881

Ligands and binding sites

  • CVW · 2-(5-methyl-1~{H}-indol-3-yl)ethanamine · ligand · 2 copies · chains A, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1880.490.8220CVW
2690.450.8215CVW

Interfaces

1 interface between chains.

  • A–C · 2359 Ų buried · 18 hydrogen bonds · protein-protein

Compared structures

  • 6F7G · Tryptophan Repressor TrpR from E.coli with 5-Methyltryptamine · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A881 · AlphaFold monomer V2.0 prediction for TRP operon repressor (P0A881) · a predicted model of the same protein · chain C against A, TM-score 0.98

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