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The crystal structure of a CYS25ALA mutant of human procathepsin S

Analyse The crystal structure of a CYS25ALA mutant of human procathepsin S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2C0Y
Type
protein
Length
308 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Procathepsin S
EC
3.4.22.27
UniProt
P25774
Pockets
1 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProcathepsin S (EC 3.4.22.27)protein30837% helix, 19% strandP25774

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11270.500.8023empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 2C0Y · The crystal structure of a CYS25ALA mutant of human procathepsin S · the same entry in another collection · chain A against A, TM-score 1.00
  • P25774 · AlphaFold monomer V2.0 prediction for cathepsin S (P25774) · a predicted model of the same protein · chain A against A, TM-score 0.99

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