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The three-dimensional structure of tyrosine phenol-lyase

Analyse The three-dimensional structure of tyrosine phenol-lyase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1TPL
Type
protein
Length
852 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine phenol-lyase
EC
4.1.99.2
UniProt
P31012
Ligands
SO4
Pockets
12 · best druggability 0.64

Structure

x-ray diffraction · 2 distinct chains · 43% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATyrosine phenol-lyase (EC 4.1.99.2)protein42643% helix, 16% strandP31012
BTyrosine phenol-lyase (EC 4.1.99.2)protein42643% helix, 18% strandP31012

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 4 copies · chains A, 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, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14040.640.7857empty
24600.620.7661SO4
33940.580.7557empty
41780.520.7828empty
51170.430.7720empty

Interfaces

1 interface between chains.

  • A–B · 1871 Ų buried · 32 hydrogen bonds · protein-protein

Compared structures

  • 1TPL · The three-dimensional structure of tyrosine phenol-lyase · the same entry in another collection · chain A against A, TM-score 1.00
  • P31012 · AlphaFold monomer V2.0 prediction for tyrosine phenol-lyase (P31012) · a predicted model of the same protein · chain B against A, TM-score 0.95

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