GL1X · GenesisL1 explorer

MolNFT v1 · #146838 · protein

Human polycsytin 2-L1

6DU8 · Polycystic kidney disease 2-like 1 protein: “Human polycsytin 2-L1”. Electron microscopy, 1 ligand (NAG), 20 pockets (best druggability 0.79). MolNFT v1 #146838 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
6DU8
Type
protein
Length
1,684 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Polycystic kidney disease 2-like 1 protein
UniProt
Q9P0L9
Ligands
NAG
Pockets
20 · best druggability 0.79

Structure

electron microscopy · 1 distinct chain · 43% helix, 10% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DPolycystic kidney disease 2-like 1 proteinprotein42143% helix, 10% strandQ9P0L9

Ligands and binding sites

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

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
13330.790.9053empty
23710.780.8854empty
31460.770.9430empty
41570.760.9329empty
55920.730.7961empty

Interfaces

6 interfaces between chains.

  • A–C · 2846 Ų buried · 13 hydrogen bonds · protein-protein
  • A–B · 2843 Ų buried · 13 hydrogen bonds · protein-protein
  • B–D · 2841 Ų buried · 13 hydrogen bonds · protein-protein
  • C–D · 2840 Ų buried · 13 hydrogen bonds · protein-protein
  • B–C · 16 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

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

Compared structures

  • 6DU8 · Human Polycsytin 2-l1 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9P0L9 · AlphaFold monomer V2.0 prediction for polycystic kidney disease 2-like 1 protein (Q9P0L9) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

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