GL1X · GenesisL1 explorer

MolNFT v1 · #180965 · protein

PEG10 ca-like C-terminal domain

7LGA · Retrotransposon-derived protein PEG10: “PEG10 ca-like C-terminal domain”. X-ray diffraction, 5 pockets (best druggability 0.76). MolNFT v1 #180965 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7LGA
Type
protein
Length
347 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Retrotransposon-derived protein PEG10
UniProt
Q86TG7
Pockets
5 · best druggability 0.76

Structure

x-ray diffraction · 4 distinct chains · 70% helix, 1% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ARetrotransposon-derived protein PEG10protein8568% helix, 1% strandQ86TG7
BRetrotransposon-derived protein PEG10protein8572% helix, 1% strandQ86TG7
DRetrotransposon-derived protein PEG10protein9168% helix, 1% strandQ86TG7
ERetrotransposon-derived protein PEG10protein8672% helix, 1% strandQ86TG7

Pockets

5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18560.760.8078empty
21410.540.8119empty
31840.490.7624empty
41220.470.7820empty
51080.460.7917empty

Interfaces

4 interfaces between chains.

  • D–E · 621 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 588 Ų buried · 16 hydrogen bonds · protein-protein
  • A–E · 484 Ų buried · 11 hydrogen bonds · protein-protein
  • B–D · 482 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 modified (engineered).

Compared structures

  • 7LGA · PEG10 CA-like C-terminal domain · the same entry in another collection · chain E against E, TM-score 1.00
  • Q86TG7 · AlphaFold monomer V2.0 prediction for retrotransposon-derived protein PEG10 (Q86TG7) · a predicted model of the same protein · chain E against A, TM-score 0.97

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.