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Crystal structure of Helicobacter pylori ATP dependent protease, FtsH ADP complex

Analyse Crystal structure of Helicobacter pylori ATP dependent protease, FtsH ADP… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2R65
Type
protein
Length
1,245 residues
Chains
5
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.3
Source
Helicobacter pylori
Molecule
Cell division protease ftsH homolog
EC
3.4.24.-
UniProt
P71408
Ligands
ADP
Pockets
13 · best druggability 0.72

Structure

x-ray diffraction · resolution 3.3 · 1 distinct chain · 40% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, ECell division protease ftsH homolog (EC 3.4.24.-)protein24940% helix, 10% strandP71408

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 5 copies · chains A, B, C, D, E

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

Pockets

13 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111120.720.7696ADP
211920.710.75101ADP
34530.710.8140empty
41230.680.9025empty
55780.680.7751empty

Interfaces

4 interfaces between chains.

  • D–E · 821 Ų buried · 10 hydrogen bonds · protein-protein
  • B–C · 778 Ų buried · 10 hydrogen bonds · protein-protein
  • A–B · 760 Ų buried · 8 hydrogen bonds · protein-protein
  • C–D · 743 Ų buried · 8 hydrogen bonds · protein-protein

Compared structures

  • 2R65 · Crystal structure of helicobacter pylori ATP dependent protease, ftsh ADP complex · the same entry in another collection · chain E against E, TM-score 1.00
  • P71408 · AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh (P71408) · a predicted model of the same protein · chain E against A, TM-score 0.92

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