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Cathepsin K complexed with T-BUTYL(1S)-1-cyclohexyl-2- oxoethylcarbamate

Analyse Cathepsin K complexed with T-BUTYL(1S)-1-cyclohexyl-2- oxoethylcarbamate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Q6K
Type: protein
Length: 215 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cathepsin K
EC: 3.4.22.38
UniProt: P43235
Ligands: TCO, SO4

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cathepsin K (EC 3.4.22.38)	protein	215	26% helix, 23% strand	P43235

Ligands and binding sites

TCO · Tert-butyl(1s)-1-cyclohexyl-2-oxoethylcarbamate · ligand · chains A
SO4 · Sulfate ion · ion · chains A

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

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

1Q6K · Cathepsin K complexed with t-butyl(1S)-1-cyclohexyl-2-oxoethylcarbamate · 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 1Q6K · PDBe 1Q6K · UniProt P43235

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