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Crystal structure of sek

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

PDB
2NTT
Type
protein
Length
434 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Staphylococcal enterotoxin K
UniProt
Q5HHK0
Ligands
CL
Pockets
5 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 21% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BStaphylococcal enterotoxin Kprotein21721% helix, 38% strandQ5HHK0

Ligands and binding sites

  • CL · Chloride ion · ion · 13 copies · chains A, B
  • EDO · 1,2-ethanediol · additive · 10 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1640.450.8214CL
21100.420.7722empty
3580.350.7814CL
4900.320.7320CL
5540.310.7622EDO

Interfaces

1 interface between chains.

  • A–B · 563 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 2NTT · Crystal Structure of SEK · the same entry in another collection · chain A against A, TM-score 1.00

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