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MolNFT v1 · #138772 · protein

Crystal structure of human proteasome-assembling chaperone PAC4

5WTQ · Proteasome assembly chaperone 4: “Crystal structure of human proteasome-assembling chaperone PAC4”. X-ray diffraction, 2 ligands (NI, CL), 3 pockets (best druggability 0.59). MolNFT v1 #138772 on GenesisL1: 3D structure, binding…

PDB
5WTQ
Type
protein
Length
433 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Proteasome assembly chaperone 4
UniProt
Q5JS54
Ligands
NI, CL
Pockets
3 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 30% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProteasome assembly chaperone 4protein11429% helix, 35% strandQ5JS54
B, DProteasome assembly chaperone 4protein10731% helix, 37% strandQ5JS54
CProteasome assembly chaperone 4protein10530% helix, 36% strandQ5JS54

Ligands and binding sites

  • NI · Nickel (II) ion · metal · 4 copies · chains A, B, C, D
  • CL · Chloride ion · ion · 4 copies · chains A, B, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14840.590.7448empty
22120.550.7828empty
32120.540.7827empty

Interfaces

3 interfaces between chains.

  • A–B · 2148 Ų buried · 28 hydrogen bonds · protein-protein
  • C–D · 2112 Ų buried · 28 hydrogen bonds · protein-protein
  • A–C · 339 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

  • 5WTQ · Crystal structure of human proteasome-assembling chaperone PAC4 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q5JS54 · AlphaFold monomer V2.0 prediction for proteasome assembly chaperone 4 (Q5JS54) · a predicted model of the same protein · chain A against A, TM-score 0.63

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