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Structural studies on a non-toxic homologue of type II rips from momordica charantia (bitter gourd)-native-3

Analyse Structural studies on a non-toxic homologue of type II rips from momordica… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ZA3
Type
protein
Length
507 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RRNA N-glycosidase
EC
3.2.2.22
UniProt
B7X8M2
Ligands
NAG, FUC, BMA
Pockets
4 · best druggability 0.65

Structure

x-ray diffraction · 2 distinct chains · 27% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARRNA N-glycosidase (EC 3.2.2.22)protein24742% helix, 22% strandB7X8M2
BRRNA N-glycosidase (EC 3.2.2.22)protein26012% helix, 36% strandB7X8M2

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains B, A
  • FUC · alpha-L-fucopyranose · sugar
  • BMA · beta-D-mannopyranose · sugar
  • EDO · 1,2-ethanediol · additive · 6 copies · chains A, B
  • GOL · Glycerol · additive · chains B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11170.650.8929empty
23240.620.7940EDO
32640.550.7642empty
41440.460.7718EDO

Interfaces

1 interface between chains.

  • A–B · 1739 Ų buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 5 disulfide, 3 glycan (disulfide, N-glycosylation).

Compared structures

  • 4ZA3 · Structural studies on a non-toxic homologue of type II RIPs from Momordica charantia… · the same entry in another collection · chain A against A, TM-score 1.00

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