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Crystal structure of trypanosoma brucei cathepsin B R91C/T223C mutant in the living cell

Analyse Crystal structure of trypanosoma brucei cathepsin B R91C/T223C mutant in the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7E3G
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 0.57

Structure

x-ray diffraction · 1 distinct chain · 26% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACysteine peptidase C (cpc) (EC 3.4.22.-)protein30826% helix, 22% strandD6XHE1

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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11450.570.8223empty
2730.330.7525empty

Modifications

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

Compared structures

  • 7E3G · Crystal structure of Trypanosoma brucei cathepsin B R91C/T223C mutant in the living cell · the same entry in another collection · chain A against A, TM-score 1.00

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