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Solution structure and dynamics of the small GTPase ralb in its active conformation: significance for effector protein binding

Analyse Solution structure and dynamics of the small GTPase ralb in its active… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2KE5
Type
protein
Length
174 residues
Chains
1
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
RAS-related protein ral-B
UniProt
P11234
Ligands
GNP, MG
Pockets
1 · best druggability 0.48

Structure

solution nmr · 1 distinct chain · 34% helix, 22% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARAS-related protein ral-Bprotein17434% helix, 22% strandP11234

Ligands and binding sites

  • GNP · Phosphoaminophosphonic acid-guanylate ester · ligand · chains A
  • MG · Magnesium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11680.480.7732GNP, MG

Compared structures

  • 2KE5 · Solution structure and dynamics of the small GTPase Ralb in its active conformation… · the same entry in another collection · chain A against A, TM-score 1.00
  • P11234 · AlphaFold monomer V2.0 prediction for RAS-related protein ral-B (P11234) · a predicted model of the same protein · chain A against A, TM-score 0.89

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