GL1X · GenesisL1 explorer

Research workbench

Dimeric form of human LLT1, a ligand for nkr-P1

Analyse Dimeric form of human LLT1, a ligand for nkr-P1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4QKH
Type
protein
Length
244 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
C-type lectin domain family 2 member D
UniProt
Q9UHP7
Ligands
NAG
Pockets
2 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 17% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AC-type lectin domain family 2 member Dprotein12317% helix, 28% strandQ9UHP7
BC-type lectin domain family 2 member Dprotein12117% helix, 32% strandQ9UHP7

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1570.580.9128empty
2500.300.7611empty

Interfaces

1 interface between chains.

  • A–B · 857 Ų buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

  • 4QKH · Dimeric form of human LLT1, a ligand for NKR-P1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9UHP7 · AlphaFold monomer V2.0 prediction for C-type lectin domain family 2 member D (Q9UHP7) · a predicted model of the same protein · chain B 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.