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TRP synthase (D60N-ipp-ser) with K+

Analyse TRP synthase (D60N-ipp-ser) with K+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BEU
Type
protein
Length
642 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tryptophan synthase
EC
4.2.1.20
UniProt
P00929, P0A2K1
Ligands
IPL, PLS, K
Pockets
5 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 18% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATryptophan synthase (EC 4.2.1.20)protein25354% helix, 13% strandP00929
BTryptophan synthase (EC 4.2.1.20)protein38948% helix, 21% strandP0A2K1

Ligands and binding sites

  • IPL · Indole-3-propanol phosphate · ligand · chains A
  • PLS · [3-hydroxy-2-methyl-5-phosphonooxymethyl-pyridin-4-ylmethyl]-serine · ligand · chains B
  • K · Potassium ion · metal · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13800.760.8672PLS
23750.670.8034IPL
3790.380.7715empty
4710.370.7819empty
5620.320.7617empty

Interfaces

1 interface between chains.

  • A–B · 1367 Ų buried · 27 hydrogen bonds · protein-protein

Compared structures

  • 1BEU · TRP synthase (D60N-ipp-ser) with K+ · the same entry in another collection · chain A against A, TM-score 1.00
  • P0A2K1 · AlphaFold monomer V2.0 prediction for tryptophan synthase beta chain (P0A2K1) · a predicted model of the same protein · chain B against A, TM-score 0.99
  • P00929 · AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (P00929) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

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