Perdeuterated tyrosine phenol-lyase from Citrobacter freundii complexed with an aminoacrylate intermediate formed from S-ethyl-L-cysteine and 4-hydroxypyridine

Structure

x-ray diffraction · resolution 2.26 · 1 distinct chain · 44% helix, 15% strand (DSSP).

Ligands and binding sites

• CQG · pyridin-4-ol · ligand · 3 copies · chains A, B
• 0JO · 2-{[(E)-{3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methylidene]amino}prop-2-enoic acid · ligand · chains A, B
• DHA · 2-amino-acrylic acid · ligand · chains A, B
• K · Potassium ion · metal · 2 copies · chains A, B
• P33 · 3,6,9,12,15,18-hexaoxaicosane-1,20-diol · additive · chains B

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

Pockets

12 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 2454 Ų buried · 36 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 modified (covalent ligand, cofactor).

Compared structures

• 6NV8 · Perdeuterated tyrosine phenol-lyase from citrobacter freundii complexed with an… · the same entry in another collection · chain A against A, TM-score 1.00
• P31013 · AlphaFold monomer V2.0 prediction for tyrosine phenol-lyase (P31013) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P31013
• Elsewhere: RCSB PDB 6NV8 · PDBe 6NV8 · UniProt P31013