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Crystal structure of the cysteine protease human cathepsin K in complex with a covalent azepanone 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: 1NL6
Type: protein
Length: 430 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cathepsin K
EC: 3.4.22.38
UniProt: P43235
Ligands: 750

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cathepsin K (EC 3.4.22.38)	protein	215	29% helix, 19% strand	P43235

Ligands and binding sites

750 · 5-(2-morpholin-4-ylethoxy)benzofuran-2-carboxylic acid ((S)-3-methyl-1-{(S)-3-oxo-1-[2-(3-pyridin-2-ylphenyl)acetyl]azepan-4-ylcarbamoyl}butyl)amide · ligand · 2 copies · chains A, B

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

Modifications

Observed in the structure: 6 disulfide, 2 covalent (disulfide, covalent ligand).

Compared structures

1NL6 · 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 1NL6 · PDBe 1NL6 · UniProt P43235

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