Research workbench
cryo-EM structure of human NKCC1
Analyse cryo-EM structure of human NKCC1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PZT
- Type
- protein
- Length
- 932 residues
- Chains
- 2
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.46
- Source
- Homo sapiens
- Molecule
- Solute carrier family 12 member 2
- UniProt
- P55011
- Pockets
- 11 · best druggability 0.79
Structure
electron microscopy · resolution 3.46 · 1 distinct chain · 67% helix, 1% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B, A | Solute carrier family 12 member 2 | protein | 466 | 67% helix, 1% strand | P55011 |
Pockets
11 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1122 | 0.79 | 0.80 | 89 | empty |
| 2 | 603 | 0.78 | 0.84 | 94 | empty |
| 3 | 287 | 0.77 | 0.90 | 55 | empty |
| 4 | 355 | 0.63 | 0.78 | 48 | empty |
| 5 | 58 | 0.44 | 0.83 | 19 | empty |
Interfaces
1 interface between chains.
- B–A · 478 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 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 P55011
- Elsewhere: RCSB PDB 6PZT · PDBe 6PZT · UniProt P55011
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