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Crystal structure of the human squalene synthase

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

PDB
3VJ9
Type
protein
Length
335 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Squalene synthase
EC
2.5.1.21
UniProt
P37268
Ligands
CA, NI
Pockets
2 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 74% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASqualene synthase (EC 2.5.1.21)protein33574% helix, 0% strandP37268

Ligands and binding sites

  • CA · Calcium ion · metal · chains A
  • NI · Nickel (II) ion · metal · 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
18260.750.7954CA
2740.430.8018empty

Compared structures

  • 3VJ9 · Crystal structure of the human squalene synthase · the same entry in another collection · chain A against A, TM-score 1.00
  • P37268 · AlphaFold monomer V2.0 prediction for squalene synthase (P37268) · a predicted model of the same protein · chain A against A, TM-score 0.99

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