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Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain (in apo form)

Analyse Crystal structure of human aminoadipate semialdehyde synthase, saccharopine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5L76
Type
protein
Length
439 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Alpha-aminoadipic semialdehyde synthase, mitochondrial
EC
1.5.1.8, 1.5.1.9
UniProt
Q9UDR5
Pockets
2 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAlpha-aminoadipic semialdehyde synthase, mitochondrial (EC 1.5.1.8, 1.5.1.9)protein43938% helix, 24% strandQ9UDR5

Ligands and binding sites

  • EDO · 1,2-ethanediol · additive · 5 copies · chains A
  • PEG · Di(hydroxyethyl)ether · additive · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17100.730.7958empty
21280.440.7719empty

Compared structures

  • 5L76 · Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase… · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UDR5 · AlphaFold monomer V2.0 prediction for alpha-aminoadipic semialdehyde synthase… · a predicted model of the same protein · chain A against A, TM-score 0.97

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