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Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution

Analyse Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1NIO
Type
protein
Length
247 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
B-luffin
EC
3.2.2.22
UniProt
P22851
Ligands
NAG
Pockets
2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AB-luffin (EC 3.2.2.22)protein24740% helix, 25% strandP22851

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11180.510.8119empty
2750.330.7415empty

Modifications

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

Compared structures

  • 1NIO · Crystal structure of beta-luffin, a ribosome inactivating protein at 2.0A resolution · the same entry in another collection · chain A against A, TM-score 1.00
  • P22851 · AlphaFold monomer V2.0 prediction for ribosome-inactivating protein luffin-B (P22851) · a predicted model of the same protein · chain A against A, TM-score 0.99

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