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Structural and biochemical characterization of HP0315 from helicobacter pylori as a vapd protein with an endoribonuclease activity

Analyse Structural and biochemical characterization of HP0315 from helicobacter pylori… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3UI3
Type
protein
Length
246 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
P19909, O05728

Structure

x-ray diffraction · 2 distinct chains.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein143—P19909, O05728
B—protein103—P19909, O05728

Compared structures

  • 3UI3 · Structural and Biochemical Characterization of HP0315 from Helicobacter pylori as a VapD… · the same entry in another collection · chain A against A, TM-score 1.00
  • O05728 · AlphaFold monomer V2.0 prediction for endoribonuclease vapd (O05728) · a predicted model of the same protein · chain B against A, TM-score 0.87
  • P19909 · AlphaFold monomer V2.0 prediction for immunoglobulin G-binding protein G (P19909) · a predicted model of the same protein · chain A against A, TM-score 0.34

Analyse

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