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Crystal structure of rhogdi K135H,K138H,K141H mutant

Analyse Crystal structure of rhogdi K135H,K138H,K141H mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2JHS
Type
protein
Length
137 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rho GDP-dissociation inhibitor 1
UniProt
P52565
Pockets
1 · best druggability 0.45

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARho GDP-dissociation inhibitor 1protein1375% helix, 56% strandP52565

Ligands and binding sites

  • FLC · Citrate anion · additive · 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
11020.450.7917empty

Compared structures

  • 2JHS · Crystal structure of rhogdi K135H,K138H,K141H mutant · the same entry in another collection · chain A against A, TM-score 1.00
  • P52565 · AlphaFold monomer V2.0 prediction for rho GDP-dissociation inhibitor 1 (P52565) · a predicted model of the same protein · chain A against A, TM-score 0.98

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