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Structure of intermediate processing form of cathepsin B1 from schistosoma mansoni

Analyse Structure of intermediate processing form of cathepsin B1 from schistosoma… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4I05
Type: protein
Length: 277 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cathepsin B-like peptidase (C01 family)
EC: 3.4.22.1
UniProt: Q8MNY2
Ligands: NA
Pockets: 2 · best druggability 0.53

Structure

x-ray diffraction · 1 distinct chain · 27% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cathepsin B-like peptidase (C01 family) (EC 3.4.22.1)	protein	277	27% helix, 22% strand	Q8MNY2

Ligands and binding sites

NA · Sodium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	198	0.53	0.78	28	empty
2	72	0.34	0.76	13	empty

Modifications

Observed in the structure: 6 disulfide, 1 modified (disulfide, oxidation).

Compared structures

4I05 · Structure of intermediate processing form of cathepsin B1 from Schistosoma mansoni · the same entry in another collection · 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 Q8MNY2
Elsewhere: RCSB PDB 4I05 · PDBe 4I05 · UniProt Q8MNY2

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