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The crystal structure of human procathepsin K

Analyse The crystal structure of human procathepsin K in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1BY8
Type
protein
Length
310 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (procathepsin K)
EC
3.4.22.38
UniProt
P43235
Pockets
3 · best druggability 0.43

Structure

x-ray diffraction · 1 distinct chain · 33% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (procathepsin K) (EC 3.4.22.38)protein31033% helix, 16% strandP43235

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1840.430.8021empty
2560.390.8015empty
31110.360.7415empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 1BY8 · The crystal structure of human procathepsin K · the same entry in another collection · chain A against A, TM-score 1.00
  • P43235 · AlphaFold monomer V2.0 prediction for cathepsin K (P43235) · a predicted model of the same protein · chain A against A, TM-score 0.98

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