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Crystal structure of the cysteine protease human cathepsin K in complex with a covalent propanone inhibitor

Analyse Crystal structure of the cysteine protease human cathepsin K in complex with a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1AU2
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.6
Source: Homo sapiens
Molecule: Cathepsin K
EC: 3.4.22.38
UniProt: P43235
Ligands: POS

Structure

x-ray diffraction · resolution 2.6 · 1 distinct chain · 28% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cathepsin K (EC 3.4.22.38)	protein	215	28% helix, 21% strand	P43235

Ligands and binding sites

POS · 1-[[(4-phenoxyphenyl)sulfonyl]amino]-3-[[N/N-(4-pyridinylcarbonyl)-L-leucyl]amino]-2-propanol · ligand · chains A

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

Modifications

Observed in the structure: 3 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

1AU2 · Crystal structure of the cysteine protease human cathepsin K in complex with a covalent… · 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 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P43235
Elsewhere: RCSB PDB 1AU2 · PDBe 1AU2 · UniProt P43235

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