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The structure of active serpin K from manduca sexta and a model for serpin-protease complex formation

Analyse The structure of active serpin K from manduca sexta and a model for… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1SEK
Type
protein
Length
376 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Serpin K
UniProt
P14754
Pockets
2 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASerpin Kprotein37633% helix, 33% strandP14754

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12880.650.8235empty
21360.590.8431empty

Compared structures

  • 1SEK · The structure of active serpin K from manduca sexta and a model for serpin-protease… · the same entry in another collection · chain A against A, TM-score 1.00
  • P14754 · AlphaFold monomer V2.0 prediction for alaserpin (P14754) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

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