GL1X · GenesisL1 explorer

Research workbench

Structure of tyrosine decarboxylase complex with plp at 1.9 ångströms resolution

Analyse Structure of tyrosine decarboxylase complex with plp at 1.9 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5HSJ
Type
protein
Length
1,201 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Putative decarboxylase
EC
4.1.1.25
UniProt
J7GQ11
Ligands
PLP
Pockets
12 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 51% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APutative decarboxylase (EC 4.1.1.25)protein60650% helix, 14% strandJ7GQ11
BPutative decarboxylase (EC 4.1.1.25)protein59552% helix, 14% strandJ7GQ11

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · 2 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, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110010.830.84122PLP
2840.750.9828empty
35680.730.8163PLP
42450.700.8544empty
51530.530.8026empty

Interfaces

1 interface between chains.

  • A–B · 6875 Ų buried · 88 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 cofactor (pyridoxal phosphate Schiff base).

Compared structures

  • 5HSJ · Structure of tyrosine decarboxylase complex with PLP at 1.9 Angstroms resolution · the same entry in another collection · chain A against A, TM-score 1.00
  • J7GQ11 · AlphaFold monomer V2.0 prediction for L-tyrosine decarboxylase (J7GQ11) · a predicted model of the same protein · chain B against A, TM-score 0.98

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.