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Solution structure of the cyclic-nucleotide binding homology domain of a kcnh channel
Analyse Solution structure of the cyclic-nucleotide binding homology domain of a kcnh… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MHF
- Type
- protein
- Length
- 135 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Uncharacterized protein
- UniProt
- F1QQX6
- Pockets
- 2 · best druggability 0.55
Structure
solution nmr · 1 distinct chain · 27% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Uncharacterized protein | protein | 135 | 27% helix, 41% strand | F1QQX6 |
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.55 | 0.83 | 21 | empty |
| 2 | 69 | 0.51 | 0.84 | 21 | empty |
Compared structures
- 2MHF · Solution structure of the cyclic-nucleotide binding homology domain of a KCNH 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 F1QQX6
- Elsewhere: RCSB PDB 2MHF · PDBe 2MHF · UniProt F1QQX6
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