Research workbench
Cryoem structure of a prokaryotic cyclic nucleotide-gated ion channel
Analyse Cryoem structure of a prokaryotic cyclic nucleotide-gated ion channel in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5V4S
- Type
- protein
- Length
- 1,548 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Transporter, cation channel family / cyclic nucleotide- binding domain multi-domain…
- UniProt
- I0XVQ9
- Pockets
- 20 · best druggability 0.80
Structure
electron microscopy · 1 distinct chain · 67% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Transporter, cation channel family / cyclic nucleotide- binding domain multi-domain protein | protein | 387 | 67% helix, 10% strand | I0XVQ9 |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 844 | 0.80 | 0.83 | 88 | empty |
| 2 | 767 | 0.74 | 0.79 | 68 | empty |
| 3 | 738 | 0.73 | 0.79 | 68 | empty |
| 4 | 536 | 0.71 | 0.80 | 57 | empty |
| 5 | 478 | 0.69 | 0.80 | 53 | empty |
Interfaces
6 interfaces between chains.
- A–D · 1602 Ų buried · 17 hydrogen bonds · protein-protein
- C–D · 1601 Ų buried · 17 hydrogen bonds · protein-protein
- B–C · 1600 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 1599 Ų buried · 16 hydrogen bonds · protein-protein
- B–D · 33 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 5V4S · CryoEM Structure of a Prokaryotic Cyclic Nucleotide-Gated Ion Channel · 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 I0XVQ9
- Elsewhere: RCSB PDB 5V4S · PDBe 5V4S · UniProt I0XVQ9
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