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Crystal structure of the human RHOA/GDP complex

Analyse Crystal structure of the human RHOA/GDP complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1FTN
Type
protein
Length
177 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transforming protein rhoa (H12)
UniProt
P61586
Ligands
GDP, MG
Pockets
2 · best druggability 0.41

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 21% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransforming protein rhoa (H12)protein17740% helix, 21% strandP61586

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · 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

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11000.410.7723MG, GDP
2670.360.7717empty

Compared structures

  • 1FTN · Crystal structure of the human RHOA/GDP complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P61586 · AlphaFold monomer V2.0 prediction for transforming protein rhoa (P61586) · a predicted model of the same protein · chain A against A, TM-score 0.96

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