MolNFT v1 · #4158 · protein

Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the active site cysteine

1DEU: “Crystal structure of human procathepsin X: a cysteine protease with the proregion covalently linked to the…”. X-ray diffraction, 2 pockets (best druggability 0.39). MolNFT v1 #4158 on GenesisL1: 3D structure, binding sites and…

PDB: 1DEU
Type: protein
Length: 536 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Procathepsin X
UniProt: Q9UBR2
Pockets: 2 · best druggability 0.39

Structure

x-ray diffraction · 2 distinct chains · 25% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Procathepsin X	protein	275	24% helix, 27% strand	Q9UBR2
B	Procathepsin X	protein	261	25% helix, 27% strand	Q9UBR2

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	80	0.39	0.78	15	empty
2	85	0.30	0.72	21	empty

Modifications

Observed in the structure: 10 disulfide (disulfide).

Compared structures

1DEU · Crystal structure of human procathepsin X: a cysteine protease with the proregion… · the same entry in another collection · chain A against A, TM-score 1.00
Q9UBR2 · AlphaFold monomer V2.0 prediction for cathepsin Z (Q9UBR2) · 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 Q9UBR2
Elsewhere: RCSB PDB 1DEU · PDBe 1DEU · UniProt Q9UBR2

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