GL1X · GenesisL1 explorer

UniProt P0A853

Tryptophanase (P0A853)

Tryptophanase (UniProt P0A853), EC 4.1.99.1: 12 experimental structures and 1 predicted model on GenesisL1, 4 ligands bound, 8 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
P0A853
Protein
Tryptophanase
EC
4.1.99.1
Experimental structures
12
Predicted models
1
Ligands
4
Pockets
8 · 2 records with a druggable one

Structures

13 records of P0A853 in the MolNFT archive: 12 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
2OQXCrystal Structure of the apo form of E. coli tryptophanase at 1.9 A resolutionx-ray diffractionA——
2OQXCrystal structure of the apo form of E. COLI tryptophanase at 1.9 a resolutionx-ray diffractionA——
2V0YCrystal structure of apo C298S tryptophanase from E.colix-ray diffractionA——
2V0YCrystal structure of apo C298S tryptophanase from E.COLIx-ray diffractionA——
2V1PCrystal Structure of the apo form of Y74F mutant E. coli tryptophanasex-ray diffractionA——
2V1PCrystal structure of the apo form of Y74F mutant E. COLI tryptophanasex-ray diffractionA——
4W1YCrystal structure of Escherichia coli Tryptophanase in 'semi-holo' formx-ray diffractionA, B——
4W1YCrystal structure of escherichia COLI tryptophanase in 'semi-holo' formx-ray diffractionA, B——
4W4HEscherichia coli tryptophanase in holo formx-ray diffractionA, B——
4W4HEscherichia COLI tryptophanase in holo formx-ray diffractionA, B——
5D8GA structural view on the dissociation of E. coli Tryptophanasex-ray diffractionACL, MG, NA, CA4 (best 0.62)
5D8GA structural view on the dissociation of E. COLI tryptophanasex-ray diffractionA——
P0A853AlphaFold monomer V2.0 prediction for tryptophanase (P0A853)predictedA—4 (best 0.66)

Ligands

  • CA · Calcium ion · in 1 record
  • CL · Chloride ion · in 1 record
  • MG · Magnesium ion · in 1 record
  • NA · Sodium ion · in 1 record

Experiment against prediction

Elsewhere

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.