Research workbench
Erythrocyte ankyrin-1 complex class 2 local refinement of AQP1 (C4 symmetry applied)
Analyse Erythrocyte ankyrin-1 complex class 2 local refinement of AQP1 (C4 symmetry… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7UZE
- Type
- protein
- Length
- 988 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Aquaporin-1
- UniProt
- P29972
- Ligands
- CLR
- Pockets
- 12 · best druggability 0.83
Structure
electron microscopy · 1 distinct chain · 70% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, B, C, A | Aquaporin-1 | protein | 247 | 70% helix, 0% strand | P29972 |
Ligands and binding sites
- CLR · Cholesterol · ligand · 4 copies · chains D, C, B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
12 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 196 | 0.83 | 0.96 | 29 | empty |
| 2 | 1071 | 0.79 | 0.81 | 104 | empty |
| 3 | 133 | 0.79 | 0.96 | 47 | empty |
| 4 | 364 | 0.64 | 0.79 | 52 | empty |
| 5 | 395 | 0.64 | 0.78 | 50 | empty |
Interfaces
6 interfaces between chains.
- D–C · 1589 Ų buried · 16 hydrogen bonds · protein-protein
- C–A · 1587 Ų buried · 17 hydrogen bonds · protein-protein
- D–B · 1584 Ų buried · 17 hydrogen bonds · protein-protein
- B–A · 1580 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 25 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (nonstandard).
Compared structures
- 7UZE · Erythrocyte ankyrin-1 complex class 2 local refinement of AQP1 (C4 symmetry applied) · the same entry in another collection · chain A against A, TM-score 1.00
- P29972 · AlphaFold monomer V2.0 prediction for aquaporin-1 (P29972) · a predicted model of the same protein · 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 P29972
- Elsewhere: RCSB PDB 7UZE · PDBe 7UZE · UniProt P29972
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