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Crystal structure of homoserine dehydrogenase in complex with L- cysteine and NAD

Analyse Crystal structure of homoserine dehydrogenase in complex with L- cysteine and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5X9D
Type
protein
Length
302 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Homoserine dehydrogenase
EC
1.1.1.3
UniProt
F9VNG5
Ligands
80F
Pockets
3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHomoserine dehydrogenase (EC 1.1.1.3)protein30238% helix, 22% strandF9VNG5

Ligands and binding sites

  • 80F · (2R)-3-[[(4S)-3-aminocarbonyl-1-[(2R,3R,4S,5R)-5-[[[[(2R,3S,4R,5R)-5-(6-aminopurin-9-yl)-3,4-bis(oxidanyl)oxolan-2-yl]methoxy-oxidanyl-phosphoryl]oxy-oxidanyl-phosphoryl]oxymethyl]-3,4-bis(oxidanyl)oxolan-2-yl]-4H-pyridin-4-yl]sulfanyl]-2-azanyl-propanoic acid · ligand · chains A
  • TLA · L(+)-tartaric acid · additive · 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
13160.690.834680F
2790.440.8018empty
3720.300.7312empty

Compared structures

  • 5X9D · Crystal structure of homoserine dehydrogenase in complex with L-cysteine and NAD · the same entry in another collection · chain A against A, TM-score 1.00

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