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Tyrosine aminotransferase from E. COLI

Analyse Tyrosine aminotransferase from E. COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3TAT
Type
protein
Length
2,382 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tyrosine aminotransferase
EC
2.6.1.57
UniProt
P04693
Ligands
PLP
Pockets
20 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 7% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FTyrosine aminotransferase (EC 2.6.1.57)protein39741% helix, 7% strandP04693

Ligands and binding sites

  • PLP · Pyridoxal-5'-phosphate · ligand · 6 copies · chains A, B, C, D, E, F

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12690.750.8847empty
21900.740.8932empty
31740.740.9030empty
42730.730.8743empty
51790.730.9030empty

Interfaces

4 interfaces between chains.

  • A–B · 3066 Ų buried · 43 hydrogen bonds · protein-protein
  • E–F · 2971 Ų buried · 40 hydrogen bonds · protein-protein
  • C–D · 2941 Ų buried · 39 hydrogen bonds · protein-protein
  • A–E · 439 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 cofactor (pyridoxal phosphate Schiff base).

Compared structures

  • 3TAT · Tyrosine aminotransferase from E. COLI · the same entry in another collection · chain A against A, TM-score 1.00
  • P04693 · AlphaFold monomer V2.0 prediction for aromatic-amino-acid aminotransferase (P04693) · a predicted model of the same protein · chain A against A, TM-score 0.98

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