Research workbench
Crystal structure of the spinach aquaporin SOPIP2;1 in a closed conformation
Analyse Crystal structure of the spinach aquaporin SOPIP2;1 in a closed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1Z98
- Type
- protein
- Length
- 502 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aquaporin
- UniProt
- Q41372
- Ligands
- CD
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, M | Aquaporin | protein | 251 | 68% helix, 4% strand | Q41372 |
Ligands and binding sites
- CD · Cadmium ion · metal · 2 copies · chains A, M
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.51 | 0.77 | 41 | CD |
| 2 | 154 | 0.46 | 0.76 | 24 | empty |
| 3 | 126 | 0.43 | 0.76 | 21 | empty |
Interfaces
1 interface between chains.
- A–M · 227 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 1Z98 · Crystal structure of the spinach aquaporin SoPIP2;1 in a closed conformation · the same entry in another collection · chain A against A, TM-score 1.00
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 Q41372
- Elsewhere: RCSB PDB 1Z98 · PDBe 1Z98 · UniProt Q41372
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