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Crystal structure of rhog and elmo complex

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

PDB
6UKA
Type
protein
Length
249 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Rho-related GTP-binding protein rhog; Engulfment and cell motility protein 2
UniProt
P84095, Q8BHL5
Ligands
GNP, MG
Pockets
1 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 35% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARho-related GTP-binding protein rhogprotein17740% helix, 27% strandP84095
BEngulfment and cell motility protein 2protein7224% helix, 36% strandQ8BHL5

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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11440.560.8228GNP, MG

Interfaces

1 interface between chains.

  • A–B · 505 Ų buried · 7 hydrogen bonds · protein-protein

Compared structures

  • 6UKA · Crystal structure of RHOG and ELMO complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P84095 · AlphaFold monomer V2.0 prediction for rho-related GTP-binding protein rhog (P84095) · a predicted model of the same protein · chain A against A, TM-score 0.99
  • Q8BHL5 · AlphaFold monomer V2.0 prediction for engulfment and cell motility protein 2 (Q8BHL5) · a predicted model of the same protein · chain B against A, TM-score 0.97

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