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Crystal structure of archaeoglobus fulgidus pelota reveals inter- domain structural plasticity

Analyse Crystal structure of archaeoglobus fulgidus pelota reveals inter- domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OBY
Type
protein
Length
633 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein pelota homolog
EC
3.1.-.-
UniProt
O29421
Pockets
6 · best druggability 0.60

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein pelota homolog (EC 3.1.-.-)protein31738% helix, 32% strandO29421
BProtein pelota homolog (EC 3.1.-.-)protein31637% helix, 29% strandO29421

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13510.600.7756empty
22660.590.7944empty
31260.420.7513empty
41330.390.7421empty
5520.300.7612empty

Interfaces

1 interface between chains.

  • A–B · 587 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 3OBY · Crystal structure of Archaeoglobus fulgidus Pelota reveals inter-domain structural… · the same entry in another collection · chain A against A, TM-score 1.00
  • O29421 · AlphaFold monomer V2.0 prediction for protein pelota homolog (O29421) · a predicted model of the same protein · chain B against A, TM-score 0.93

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