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Crystal structure of AMP-bound saccharopine dehydrogenase (L-lys forming) from saccharomyces cerevisiae

Analyse Crystal structure of AMP-bound saccharopine dehydrogenase (L-lys forming) from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2QRK
Type
protein
Length
365 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Saccharopine dehydrogenase [NAD+, L-lysine-forming
EC
1.5.1.7
UniProt
P38998
Ligands
AMP
Pockets
3 · best druggability 0.64

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASaccharopine dehydrogenase [NAD+, L-lysine-forming (EC 1.5.1.7)protein36538% helix, 13% strandP38998

Ligands and binding sites

  • AMP · Adenosine monophosphate · ligand · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15550.640.7539empty
2590.340.7716empty
3580.320.7617AMP

Compared structures

  • 2QRK · Crystal Structure of AMP-bound Saccharopine Dehydrogenase (L-Lys Forming) from… · the same entry in another collection · chain A against A, TM-score 1.00
  • P38998 · AlphaFold monomer V2.0 prediction for saccharopine dehydrogenase [NAD(+)… · a predicted model of the same protein · chain A against A, TM-score 0.99

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