MolNFT v1 · #176970 · protein

Crystal structure of trypanosoma brucei cathepsin B R91C/T223C mutant

7E3E · Cysteine peptidase C (cpc): “Crystal structure of trypanosoma brucei cathepsin B R91C/T223C mutant”. X-ray diffraction, 2 ligands (NAG, BMA), 2 pockets (best druggability 0.54). MolNFT v1 #176970 on GenesisL1: 3D structure, binding…

PDB: 7E3E
Type: protein
Length: 308 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cysteine peptidase C (cpc)
EC: 3.4.22.-
UniProt: D6XHE1
Ligands: NAG, BMA
Pockets: 2 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 25% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cysteine peptidase C (cpc) (EC 3.4.22.-)	protein	308	25% helix, 24% strand	D6XHE1

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
BMA · beta-D-mannopyranose · sugar

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	153	0.54	0.81	24	empty
2	88	0.33	0.74	24	empty

Modifications

Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

7E3E · Crystal structure of Trypanosoma brucei cathepsin B R91C/T223C mutant · 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 D6XHE1
Elsewhere: RCSB PDB 7E3E · PDBe 7E3E · UniProt D6XHE1

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