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crystal structure of alpha-momorcharin in complex with cAMP

Analyse crystal structure of alpha-momorcharin in complex with cAMP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LOQ
Type
protein
Length
246 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.331
Source
Momordica charantia
Molecule
Ribosome-inactivating protein momordin I
EC
3.2.2.22
UniProt
P16094
Ligands
CMP
Pockets
2 · best druggability 0.49

Structure

x-ray diffraction · resolution 1.331 · 1 distinct chain · 42% helix, 25% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARibosome-inactivating protein momordin I (EC 3.2.2.22)protein24642% helix, 25% strandP16094

Ligands and binding sites

  • CMP · Adenosine-3',5'-cyclic-monophosphate · ligand · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11350.490.7920CMP
21000.410.7716empty

Compared structures

  • 6LOQ · Crystal structure of alpha-momorcharin in complex with camp · the same entry in another collection · chain A against A, TM-score 1.00
  • P16094 · AlphaFold monomer V2.0 prediction for ribosome-inactivating protein momordin I (P16094) · a predicted model of the same protein · chain A against A, TM-score 1.00

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