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Crystal structure of the complex of type I ribosome inactivating protein in complex with mycolic acid at 1.8 a resolution

Analyse Crystal structure of the complex of type I ribosome inactivating protein in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3U8F
Type
protein
Length
246 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ribosome inactivating protein
EC
3.2.2.22
UniProt
D9J2T9
Ligands
FGM, NAG
Pockets
3 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibosome inactivating protein (EC 3.2.2.22)protein24643% helix, 25% strandD9J2T9

Ligands and binding sites

  • FGM · (2R,3R)-2-hexyl-3-hydroxytridecanoic acid · ligand · chains A
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A
  • GOL · Glycerol · additive · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11440.490.7819FGM
2750.330.7515empty
3500.250.7314empty

Modifications

Observed in the structure: 1 glycan (N-glycosylation).

Compared structures

  • 3U8F · Crystal structure of the complex of type I Ribosome inactivating protein in complex with… · the same entry in another collection · chain A against A, TM-score 1.00

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