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).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Polycystic kidney disease 2-like 1 protein | protein | 421 | 43% helix, 10% strand | Q9P0L9 |
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 333 | 0.79 | 0.90 | 53 | empty |
| 2 | 371 | 0.78 | 0.88 | 54 | empty |
| 3 | 146 | 0.77 | 0.94 | 30 | empty |
| 4 | 157 | 0.76 | 0.93 | 29 | empty |
| 5 | 592 | 0.73 | 0.79 | 61 | empty |
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
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9P0L9
- Elsewhere: RCSB PDB 6DU8 · PDBe 6DU8 · UniProt Q9P0L9
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