Research workbench
1.15 ångström crystal structure of P.PASTORIS aquaporin, AQY1, in a closed conformation at pH 3.5
Analyse 1.15 ångström crystal structure of P.PASTORIS aquaporin, AQY1, in a closed… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2W2E
- Type
- protein
- Length
- 263 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aquaporin PIP2-7 7
- UniProt
- F2QVG4
- Ligands
- CL
- Pockets
- 2 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aquaporin PIP2-7 7 | protein | 263 | 68% helix, 0% strand | F2QVG4 |
Ligands and binding sites
- CL · Chloride ion · ion · 3 copies · chains A
- BOG · octyl beta-D-glucopyranoside · additive · 6 copies · chains A
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.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 171 | 0.51 | 0.78 | 28 | empty |
| 2 | 54 | 0.30 | 0.75 | 15 | empty |
Compared structures
- 2W2E · 1.15 Angstrom crystal structure of P.pastoris aquaporin, Aqy1, 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 F2QVG4
- Elsewhere: RCSB PDB 2W2E · PDBe 2W2E · UniProt F2QVG4
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.