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Crystal structure of pentad mutant gapr-1

Analyse Crystal structure of pentad mutant gapr-1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5VHG
Type
protein
Length
150 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Golgi-associated plant pathogenesis-related protein 1
UniProt
Q9H4G4
Ligands
SO4
Pockets
1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 45% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGolgi-associated plant pathogenesis-related protein 1protein15045% helix, 17% strandQ9H4G4

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 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
1660.340.7715empty

Compared structures

  • 5VHG · Crystal structure of pentad mutant GAPR-1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9H4G4 · AlphaFold monomer V2.0 prediction for golgi-associated plant pathogenesis-related protein… · a predicted model of the same protein · chain A against A, TM-score 0.97

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