GL1X · GenesisL1 explorer

MolNFT v1 · #163832 · protein

Structure of a functional monomeric properdin lacking TSR3

6SEJ: “Structure of a functional monomeric properdin lacking TSR3”. X-ray diffraction, 4 ligands (MAN, FUC, BGC), 3 pockets (best druggability 0.50). MolNFT v1 #163832 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6SEJ
Type
protein
Length
385 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Properdin
UniProt
P27918
Ligands
MAN, FUC, BGC, NAG
Pockets
3 · best druggability 0.50

Structure

x-ray diffraction · 2 distinct chains · 4% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProperdinprotein1652% helix, 38% strandP27918
BProperdinprotein2205% helix, 34% strandP27918

Ligands and binding sites

  • MAN · alpha-D-mannopyranose · sugar · 12 copies · chains A, B
  • FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B
  • BGC · beta-D-glucopyranose · sugar · 3 copies · chains A, B
  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12190.500.7628empty
22070.500.7625empty
3790.380.7721empty

Interfaces

1 interface between chains.

  • A–B · 1155 Ų buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 19 disulfide, 16 glycan (disulfide, C-mannosylation, O-glycosylation, N-glycosylation).

Compared structures

  • 6SEJ · Structure of a functional monomeric properdin lacking TSR3 · the same entry in another collection · chain A against A, TM-score 1.00
  • P27918 · AlphaFold monomer V2.0 prediction for properdin (P27918) · a predicted model of the same protein · chain A against A, TM-score 0.83

Analyse

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