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Crystal structure of lysn, alpha-aminoadipate aminotransferase (complexed with N-(5'-phosphopyridoxyl)-L-leucine), from thermus thermophilus HB27

Analyse Crystal structure of lysn, alpha-aminoadipate aminotransferase (complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Z1Y
Type
protein
Length
783 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-aminodipate aminotransferase
EC
2.6.1.39
UniProt
Q72LL6
Ligands
LEU, PLP
Pockets
7 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-aminodipate aminotransferase (EC 2.6.1.39)protein38948% helix, 15% strandQ72LL6
BAlpha-aminodipate aminotransferase (EC 2.6.1.39)protein39448% helix, 15% strandQ72LL6

Ligands and binding sites

  • LEU · Leucine · ligand · 2 copies · chains A, B
  • 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11060.780.9726LEU, PLP
21130.770.9627LEU, PLP
3970.660.9119empty
42800.570.7747empty
51380.390.7326empty

Interfaces

1 interface between chains.

  • A–B · 3912 Ų buried · 63 hydrogen bonds · protein-protein

Compared structures

  • 2Z1Y · Crystal structure of LysN, alpha-aminoadipate aminotransferase (complexed with… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q72LL6 · AlphaFold monomer V2.0 prediction for 2-aminoadipate transaminase (Q72LL6) · a predicted model of the same protein · chain A against A, TM-score 0.98

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