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Crystal structure of arabidopsis thaliana hct

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

PDB
5KJS
Type
protein
Length
429 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Shikimate O-hydroxycinnamoyltransferase
EC
2.3.1.133
UniProt
Q9FI78
Pockets
6 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AShikimate O-hydroxycinnamoyltransferase (EC 2.3.1.133)protein42928% helix, 23% strandQ9FI78

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19310.840.8580empty
21360.610.8525empty
31050.420.7721empty
4700.370.7718empty
5630.300.7518empty

Modifications

Observed in the structure: 12 modified (engineered).

Compared structures

  • 5KJS · Crystal Structure of Arabidopsis thaliana HCT · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9FI78 · AlphaFold monomer V2.0 prediction for shikimate O-hydroxycinnamoyltransferase (Q9FI78) · a predicted model of the same protein · chain A against A, TM-score 0.99

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