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A structural view on the dissociation of E. COLI tryptophanase

Analyse A structural view on the dissociation of E. COLI tryptophanase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5D8G
Type
protein
Length
465 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tryptophanase
EC
4.1.99.1
UniProt
P0A853
Ligands
MG, NA, CA, CL
Pockets
4 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATryptophanase (EC 4.1.99.1)protein46546% helix, 14% strandP0A853

Ligands and binding sites

  • MG · Magnesium ion · metal · 3 copies · chains A
  • NA · Sodium ion · metal · chains A
  • CA · Calcium ion · metal · chains A
  • CL · Chloride ion · ion · chains A
  • EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A

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

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12610.620.8026empty
23940.600.7636empty
33300.560.7539EPE
41960.530.7828empty

Modifications

Observed in the structure: 2 modified (artifact).

Compared structures

  • 5D8G · A structural view on the dissociation of E. coli Tryptophanase · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A853 · AlphaFold monomer V2.0 prediction for tryptophanase (P0A853) · a predicted model of the same protein · chain A against A, TM-score 0.87

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