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Akirin2 bound human proteasome

Analyse Akirin2 bound human proteasome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7NHT
Type
protein
Length
3,222 residues
Chains
16
Method
electron microscopy
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.2
Source
Homo sapiens
Molecule
Proteasome subunit alpha type-2; Proteasome subunit alpha type-4; Proteasome subunit…
EC
3.4.25.1
UniProt
P25787, P25789, O14818, P28066, P25786, P25788, P60900, Q99436, P49720, P49721, P28074, P20618, P28070, P28072, Q53H80
Ligands
K
Pockets
20 · best druggability 0.84

Structure

electron microscopy · resolution 3.2 · 16 distinct chains · 36% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProteasome subunit alpha type-2protein23136% helix, 27% strandP25787
BProteasome subunit alpha type-4protein24839% helix, 26% strandP25789
CProteasome subunit alpha type-7protein23741% helix, 25% strandO14818
DProteasome subunit alpha type-5protein24131% helix, 26% strandP28066
EProteasome subunit alpha type-1protein23637% helix, 25% strandP25786
FProteasome subunit alpha type-3protein24237% helix, 27% strandP25788
GProteasome subunit alpha type-6protein24240% helix, 25% strandP60900
HProteasome subunit beta type-7 (EC 3.4.25.1)protein22030% helix, 35% strandQ99436
IProteasome subunit beta type-3 (EC 3.4.25.1)protein20431% helix, 29% strandP49720
JProteasome subunit beta type-2 (EC 3.4.25.1)protein19634% helix, 34% strandP49721
KProteasome subunit beta type-5 (EC 3.4.25.1)protein20136% helix, 33% strandP28074
LProteasome subunit beta type-1 (EC 3.4.25.1)protein21329% helix, 31% strandP20618
MProteasome subunit beta type-4 (EC 3.4.25.1)protein21635% helix, 32% strandP28070
NProteasome subunit beta type-6 (EC 3.4.25.1)protein20334% helix, 33% strandP28072
cAkirin-2protein4869% helix, 2% strandQ53H80
dAkirin-2protein4480% helix, 2% strandQ53H80

Ligands and binding sites

  • K · Potassium ion · metal · 3 copies · chains G, L, N

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13540.840.9349empty
210160.800.8195empty
39380.770.80101empty
411170.760.78118empty
58910.750.78106empty

Interfaces

49 interfaces between chains.

  • H–I · 1693 Ų buried · 30 hydrogen bonds · protein-protein
  • C–D · 1543 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 1530 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 1500 Ų buried · 24 hydrogen bonds · protein-protein
  • A–G · 1454 Ų buried · 19 hydrogen bonds · protein-protein

Compared structures

  • 7NHT · AKIRIN2 bound human proteasome · the same entry in another collection · chain K against K, TM-score 1.00

Analyse

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