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Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor

Analyse Crystal structure of the FP domain of Human PI31 Proteasome Inhibitor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4OUH
Type
protein
Length
591 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2
Source
Homo sapiens
Molecule
Proteasome inhibitor PI31 subunit
UniProt
Q92530
Pockets
4 · best druggability 0.73

Structure

x-ray diffraction · resolution 2 · 4 distinct chains · 37% helix, 27% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProteasome inhibitor PI31 subunitprotein14938% helix, 27% strandQ92530
BProteasome inhibitor PI31 subunitprotein14838% helix, 26% strandQ92530
CProteasome inhibitor PI31 subunitprotein14733% helix, 27% strandQ92530
DProteasome inhibitor PI31 subunitprotein14738% helix, 27% strandQ92530

Pockets

4 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111780.730.77104empty
21980.530.7824empty
31690.510.7824empty
41970.500.7622empty

Interfaces

5 interfaces between chains.

  • A–B · 635 Ų buried · 11 hydrogen bonds · protein-protein
  • C–D · 625 Ų buried · 11 hydrogen bonds · protein-protein
  • B–C · 169 Ų buried · 1 hydrogen bond · protein-protein
  • A–C · 160 Ų buried · 0 hydrogen bonds · protein-protein
  • B–D · 94 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 4OUH · Crystal structure of the fp domain of human PI31 proteasome inhibitor · the same entry in another collection · chain D against D, TM-score 1.00
  • Q92530 · AlphaFold monomer V2.0 prediction for proteasome inhibitor PI31 subunit (Q92530) · a predicted model of the same protein · chain C against A, TM-score 0.97

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