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X-ray crystal structure of chalcone synthase from freesia hybrida

Analyse X-ray crystal structure of chalcone synthase from freesia hybrida in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4WUM
Type
protein
Length
1,556 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Chalcone synthase
EC
2.3.1.74
UniProt
G3FJ87
Pockets
11 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DChalcone synthase (EC 2.3.1.74)protein38943% helix, 23% strandG3FJ87

Pockets

11 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12870.760.8849empty
22990.750.8747empty
37520.740.8083empty
42790.720.8646empty
52930.720.8547empty

Interfaces

6 interfaces between chains.

  • C–D · 3098 Ų buried · 64 hydrogen bonds · protein-protein
  • A–B · 3087 Ų buried · 65 hydrogen bonds · protein-protein
  • A–C · 501 Ų buried · 2 hydrogen bonds · protein-protein
  • B–D · 336 Ų buried · 3 hydrogen bonds · protein-protein
  • A–D · 58 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 4WUM · X-ray crystal structure of Chalcone Synthase from Freesia hybrida · the same entry in another collection · chain A against A, TM-score 1.00

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