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Structure of a K245A mutant of L-tyrosine decarboxylase from methanocaldococcus jannaschii complexed with L-tyr: external aldimine form

Analyse Structure of a K245A mutant of L-tyrosine decarboxylase from methanocaldococcus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LDS
Type
protein
Length
382 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
L-TYROSINE/L-aspartate decarboxylase
EC
4.1.1.11, 4.1.1.25
UniProt
Q60358
Ligands
0PR, SO4
Pockets
4 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 47% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AL-TYROSINE/L-aspartate decarboxylase (EC 4.1.1.11, 4.1.1.25)protein38247% helix, 13% strandQ60358

Ligands and binding sites

  • 0PR · N-({3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl}methyl)-L-tyrosine · ligand · chains A
  • SO4 · Sulfate ion · ion · 2 copies · chains A
  • GOL · Glycerol · additive · 4 copies · chains A

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

Pockets

4 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1630.490.8520empty
21270.480.79240PR
3780.330.7520empty
4550.320.7715empty

Modifications

Observed in the structure: 1 modified (cofactor).

Compared structures

  • 6LDS · Structure of a K245A mutant of L-tyrosine decarboxylase from Methanocaldococcus… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q60358 · AlphaFold monomer V2.0 prediction for L-TYROSINE/L-aspartate decarboxylase (Q60358) · a predicted model of the same protein · chain A against A, TM-score 1.00

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