Tyrosine 447 of protocatechuate 3,4-dioxygenase controls efficient progress through catalysis

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 30% strand (DSSP).

Ligands and binding sites

• FE · Fe (III) ion · metal · 6 copies · chains M, N, O, P, Q, R
• CL · Chloride ion · ion · 9 copies · chains M, N, O, P, Q, R
• SO4 · Sulfate ion · ion · 6 copies · chains A, B, C, D, E, F
• BME · Beta-mercaptoethanol · additive · 32 copies · chains A, M, N, B, R, C, O, E, D, P, Q, F
• TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 5 copies · chains A, B, D, E, F
• GOL · Glycerol · additive · 2 copies · chains M, C

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

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Interfaces

35 interfaces between chains.

• F–R · 3753 Ų buried · 65 hydrogen bonds · protein-protein
• B–N · 3723 Ų buried · 65 hydrogen bonds · protein-protein
• C–O · 3719 Ų buried · 66 hydrogen bonds · protein-protein
• E–Q · 3706 Ų buried · 65 hydrogen bonds · protein-protein
• D–P · 3665 Ų buried · 65 hydrogen bonds · protein-protein

Compared structures

• 3LKT · Tyrosine 447 of Protocatechuate 3,4-Dioxygenase Controls Efficient Progress Through… · the same entry in another collection · chain R against R, 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 P00436
• Every structure of UniProt P00437
• Elsewhere: RCSB PDB 3LKT · PDBe 3LKT · UniProt P00436 · UniProt P00437