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Model of ribosome-bound archaeal pelota and ABCE1

Analyse Model of ribosome-bound archaeal pelota and ABCE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3J15
Type
protein
Length
950 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein pelota; ABC transporter ATP-binding protein
EC
3.1.-.-
UniProt
Q5JIB9
Ligands
ADP, SF4
Pockets
14 · best druggability 0.69

Structure

electron microscopy · 2 distinct chains · 33% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein pelota (EC 3.1.-.-)protein35734% helix, 20% strandQ5JIB9
BABC transporter ATP-binding proteinprotein59333% helix, 20% strand—

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains B
  • SF4 · Iron/sulfur cluster · ligand · 2 copies · chains B

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

Pockets

14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17690.690.7671ADP
2970.610.8721empty
33150.570.7735ADP
42080.440.7323empty
51210.420.7614empty

Interfaces

1 interface between chains.

  • A–B · 367 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent, 1 disulfide (covalent ligand, disulfide).

Compared structures

  • 3J15 · Model of ribosome-bound archaeal Pelota and ABCE1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5JIB9 · AlphaFold monomer V2.0 prediction for protein pelota homolog (Q5JIB9) · a predicted model of the same protein · chain A against A, TM-score 0.50

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