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Human cathepsin S with inhibitor cra-16981

Analyse Human cathepsin S with inhibitor cra-16981 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2G7Y
Type
protein
Length
435 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Cathepsin S
EC
3.4.22.27
UniProt
P25774
Ligands
MO9
Pockets
2 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACathepsin S (EC 3.4.22.27)protein21729% helix, 24% strandP25774
BCathepsin S (EC 3.4.22.27)protein21828% helix, 24% strandP25774

Ligands and binding sites

  • MO9 · (1R)-2-[(cyanomethyl)amino]-1-({[2-(difluoromethoxy)benzyl]sulfonyl}methyl)-2-oxoethyl morpholine-4-carboxylate · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15310.710.8062MO9
2660.290.7318empty

Interfaces

1 interface between chains.

  • A–B · 780 Ų buried · 7 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

  • 2G7Y · Human Cathepsin S with inhibitor CRA-16981 · the same entry in another collection · chain B against B, 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 1.00

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