Research workbench
TRIP8B-1A#206-567 interacting with the carboxy-terminal seven residues of HCN2
Analyse TRIP8B-1A#206-567 interacting with the carboxy-terminal seven residues of HCN2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EQF
- Type
- protein
- Length
- 287 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- PEX5-related protein; POTASSIUM/SODIUM hyperpolarization-activated cyclic…
- UniProt
- Q8C437, O88703
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 72% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | PEX5-related protein | protein | 281 | 74% helix, 0% strand | Q8C437 |
| B | POTASSIUM/SODIUM hyperpolarization-activated cyclic nucleotide-gated channel 2 | protein | 6 | 0% helix, 0% strand | O88703 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 250 | 0.64 | 0.82 | 32 | empty |
| 2 | 63 | 0.52 | 0.85 | 13 | empty |
| 3 | 91 | 0.33 | 0.73 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 532 Ų buried · 14 hydrogen bonds · protein-protein
Compared structures
- 4EQF · Trip8b-1a#206-567 interacting with the carboxy-terminal seven residues of HCN2 · the same entry in another collection · chain A against A, TM-score 1.00
- Q8C437 · AlphaFold monomer V2.0 prediction for PEX5-related protein (Q8C437) · a predicted model of the same protein · chain A against A, TM-score 0.99
- O88703 · AlphaFold monomer V2.0 prediction for POTASSIUM/SODIUM hyperpolarization-activated cyclic… · a predicted model of the same protein · chain B against A, TM-score 0.79
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 Q8C437
- Every structure of UniProt O88703
- Elsewhere: RCSB PDB 4EQF · PDBe 4EQF · UniProt Q8C437 · UniProt O88703
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