Research workbench
X-ray structure of human aquaporin 2 crystallized on a silicon chip
Analyse X-ray structure of human aquaporin 2 crystallized on a silicon chip in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6QF5
- Type
- protein
- Length
- 900 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aquaporin-2
- UniProt
- P41181
- Ligands
- CD
- Pockets
- 11 · best druggability 0.68
Structure
x-ray diffraction · 4 distinct chains · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Aquaporin-2 | protein | 228 | 69% helix, 0% strand | P41181 |
| B | Aquaporin-2 | protein | 230 | 70% helix, 0% strand | P41181 |
| C | Aquaporin-2 | protein | 222 | 71% helix, 0% strand | P41181 |
| D | Aquaporin-2 | protein | 220 | 70% helix, 0% strand | P41181 |
Ligands and binding sites
- CD · Cadmium ion · metal · 3 copies · chains B, A, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 389 | 0.68 | 0.81 | 66 | CD |
| 2 | 559 | 0.66 | 0.77 | 52 | empty |
| 3 | 386 | 0.66 | 0.80 | 58 | empty |
| 4 | 343 | 0.64 | 0.79 | 26 | empty |
| 5 | 384 | 0.62 | 0.77 | 50 | empty |
Interfaces
6 interfaces between chains.
- B–C · 1840 Ų buried · 11 hydrogen bonds · protein-protein
- A–D · 1810 Ų buried · 9 hydrogen bonds · protein-protein
- A–C · 1764 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 1695 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 131 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
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 P41181
- Elsewhere: RCSB PDB 6QF5 · PDBe 6QF5 · UniProt P41181
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