GL1X · GenesisL1 explorer

MolNFT v2 · #188135 · protein

Akirin2 bound human proteasome

7NHT · Proteasome subunit alpha type-2: “Akirin2 bound human proteasome”. Electron microscopy at 3.2, 1 ligand (K), 20 pockets (best druggability 0.84). MolNFT v2 #188135 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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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