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Crystal structure of uninhibited human cathepsin K at 1.62 ångström resolution

Analyse Crystal structure of uninhibited human cathepsin K at 1.62 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5TUN
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
Pockets: 1 · best druggability 0.37

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cathepsin K (EC 3.4.22.38)	protein	215	30% helix, 22% strand	P43235

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.37	0.79	21	empty

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

5TUN · Crystal structure of uninhibited human Cathepsin K at 1.62 Angstrom resolution · 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 1.00

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 5TUN · PDBe 5TUN · UniProt P43235

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