GL1X · GenesisL1 explorer

Research workbench

Crystal structure of yersinia AFP18-modified rhoa

Analyse Crystal structure of yersinia AFP18-modified rhoa in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5A0F
Type
protein
Length
178 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Transforming protein rhoa
UniProt
P61586
Ligands
GDP, NDG, SO4

Structure

x-ray diffraction · 1 distinct chain · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATransforming protein rhoaprotein17838% helix, 24% strandP61586

Ligands and binding sites

  • GDP · Guanosine-5'-diphosphate · ligand · chains A
  • NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · chains A
  • SO4 · Sulfate ion · ion · chains A

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

Modifications

Observed in the structure: 1 glycan (glycosylation).

Compared structures

  • 5A0F · Crystal structure of Yersinia Afp18-modified RhoA · 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 0.91

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.