Research workbench
Room temperature structure of pichia pastoris aquaporin at 1.3 a
Analyse Room temperature structure of pichia pastoris aquaporin at 1.3 a in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5BN2
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- AQY1 protein
- UniProt
- F2QVG4
- Ligands
- CA, CL
- Pockets
- 1 · best druggability 0.51
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | AQY1 protein | protein | 260 | 68% helix, 0% strand | F2QVG4 |
Ligands and binding sites
- CA · Calcium ion · metal · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- BOG · octyl beta-D-glucopyranoside · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 199 | 0.51 | 0.77 | 27 | empty |
Compared structures
- 5BN2 · Room Temperature Structure of Pichia pastoris aquaporin at 1.3 A · 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 5BN2 · PDBe 5BN2 · UniProt F2QVG4
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