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Crystal structure of human aminoadipate semialdehyde synthase, saccharopine dehydrogenase domain with proline bound.

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
5O1O
Type
protein
Length
874 residues
Chains
2
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
Ligands
PRO
Pockets
5 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 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
BAlpha-aminoadipic semialdehyde synthase, mitochondrial (EC 1.5.1.8, 1.5.1.9)protein43538% helix, 25% strandQ9UDR5

Ligands and binding sites

  • PRO · Proline · ligand · 2 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19080.730.7789EDO, PRO
29010.730.7788PRO
31850.530.7923empty
41300.470.7822empty
5690.320.7617empty

Interfaces

1 interface between chains.

  • A–B · 1110 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 5O1O · 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 0.93

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