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MolNFT v1 · #187252 · protein

The crystal structure of human ISG15

7S6P · Ubiquitin-like protein ISG15: “The crystal structure of human ISG15”. X-ray diffraction, 9 pockets (best druggability 0.71). MolNFT v1 #187252 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7S6P
Type
protein
Length
903 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Ubiquitin-like protein ISG15
UniProt
P05161
Pockets
9 · best druggability 0.71

Structure

x-ray diffraction · 4 distinct chains · 25% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, EUbiquitin-like protein ISG15protein15125% helix, 33% strandP05161
BUbiquitin-like protein ISG15protein15225% helix, 34% strandP05161
DUbiquitin-like protein ISG15protein15025% helix, 32% strandP05161
FUbiquitin-like protein ISG15protein14826% helix, 34% strandP05161

Pockets

9 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17710.710.7776empty
27430.700.7779empty
36780.700.7750empty
46250.690.7853empty
56600.690.7758empty

Interfaces

12 interfaces between chains.

  • A–B · 973 Ų buried · 3 hydrogen bonds · protein-protein
  • C–D · 964 Ų buried · 5 hydrogen bonds · protein-protein
  • E–F · 948 Ų buried · 3 hydrogen bonds · protein-protein
  • B–C · 272 Ų buried · 5 hydrogen bonds · protein-protein
  • A–D · 260 Ų buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

  • 7S6P · The crystal structure of human ISG15 · the same entry in another collection · chain F against F, TM-score 1.00
  • P05161 · AlphaFold monomer V2.0 prediction for ubiquitin-like protein ISG15 (P05161) · a predicted model of the same protein · chain A against A, TM-score 0.87

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