Research workbench
Potassium channel KCSA(M96V)-Fab complex in kcl
Analyse Potassium channel KCSA(M96V)-Fab complex in kcl in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NLJ
- Type
- protein
- Length
- 533 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antibody Fab fragment light chain; Antibody Fab fragment heavy chain; Voltage-gated…
- UniProt
- P0A334
- Ligands
- DGA, K
- Pockets
- 6 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 18% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Antibody Fab fragment light chain | protein | 212 | 6% helix, 51% strand | — |
| B | Antibody Fab fragment heavy chain | protein | 218 | 4% helix, 50% strand | — |
| C | Voltage-gated potassium channel | protein | 103 | 74% helix, 0% strand | P0A334 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 700 | 0.67 | 0.75 | 57 | empty |
| 2 | 69 | 0.54 | 0.87 | 19 | empty |
| 3 | 58 | 0.48 | 0.85 | 20 | empty |
| 4 | 51 | 0.44 | 0.84 | 14 | empty |
| 5 | 133 | 0.44 | 0.76 | 26 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1718 Ų buried · 20 hydrogen bonds · protein-protein
- B–C · 457 Ų buried · 11 hydrogen bonds · protein-protein
- A–C · 425 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 2NLJ · Potassium Channel KcsA(M96V)-Fab complex in KCl · 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 P0A334
- Elsewhere: RCSB PDB 2NLJ · PDBe 2NLJ · UniProt P0A334
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