Research workbench
Structure of human prestin in the presence of nacl
Analyse Structure of human prestin in the presence of nacl in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LGU
- Type
- protein
- Length
- 1,360 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Prestin
- UniProt
- P58743
- Ligands
- D10, D12, HP6, C14, CLR, CL
- Pockets
- 20 · best druggability 0.86
Structure
electron microscopy · 1 distinct chain · 63% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Prestin | protein | 680 | 63% helix, 6% strand | P58743 |
Ligands and binding sites
- D10 · Decane · ligand · 36 copies · chains A, B
- D12 · Dodecane · ligand · 10 copies · chains A, B
- HP6 · Heptane · ligand · 4 copies · chains A, B
- C14 · Tetradecane · ligand · 4 copies · chains A, B
- CLR · Cholesterol · ligand · 2 copies · chains A, B
- CL · Chloride ion · ion · 2 copies · chains A, B
- OCT · N-octane · additive · 50 copies · chains A, B
- HEX · Hexane · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 9 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 849 | 0.86 | 0.88 | 68 | empty |
| 2 | 624 | 0.70 | 0.78 | 66 | empty |
| 3 | 176 | 0.67 | 0.86 | 33 | empty |
| 4 | 177 | 0.66 | 0.86 | 35 | empty |
| 5 | 329 | 0.65 | 0.81 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 4002 Ų buried · 54 hydrogen bonds · protein-protein
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 P58743
- Elsewhere: RCSB PDB 7LGU · PDBe 7LGU · UniProt P58743
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