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Crystal structure of tryptophan synthase a-subunit from thermus thermophilus HB8

Analyse Crystal structure of tryptophan synthase a-subunit from thermus thermophilus HB8 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1UJP
Type
protein
Length
243 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tryptophan synthase alpha chain
EC
4.2.1.20
UniProt
P16608
Pockets
1 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATryptophan synthase alpha chain (EC 4.2.1.20)protein24351% helix, 15% strandP16608

Ligands and binding sites

  • CIT · Citric acid · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12240.620.8231CIT

Compared structures

  • 1UJP · Crystal Structure of Tryptophan Synthase A-Subunit From Thermus thermophilus HB8 · the same entry in another collection · chain A against A, TM-score 1.00
  • P16608 · AlphaFold monomer V2.0 prediction for tryptophan synthase alpha chain (P16608) · a predicted model of the same protein · chain A against A, TM-score 0.97

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