Research workbench
Crystal structure of DLN1
Analyse Crystal structure of DLN1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5DI0
- Type
- protein
- Length
- 636 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Natterin-like protein
- UniProt
- Q5CZR5
- Ligands
- CL
- Pockets
- 11 · best druggability 0.50
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 64% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Natterin-like protein | protein | 318 | 2% helix, 64% strand | Q5CZR5 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
- EDO · 1,2-ethanediol · additive · 12 copies · chains A, B
- PEG · Di(hydroxyethyl)ether · additive · 8 copies · chains A, B
- PGE · Triethylene glycol · additive · 7 copies · chains A, B
- PG4 · Tetraethylene glycol · additive · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 102 | 0.50 | 0.81 | 24 | PG4 |
| 2 | 94 | 0.49 | 0.82 | 23 | PGE |
| 3 | 92 | 0.41 | 0.78 | 20 | PG4 |
| 4 | 99 | 0.40 | 0.77 | 19 | empty |
| 5 | 119 | 0.37 | 0.73 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 1606 Ų buried · 22 hydrogen bonds · protein-protein
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 Q5CZR5
- Elsewhere: RCSB PDB 5DI0 · PDBe 5DI0 · UniProt Q5CZR5
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