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NMR solution structure of the chemosensory protein CSP2 from moth mamestra brassicae
Analyse NMR solution structure of the chemosensory protein CSP2 from moth mamestra… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1K19
- Type
- protein
- Length
- 112 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chemosensory protein CSP2
- UniProt
- Q9NG96
- Pockets
- 2 · best druggability 0.78
Structure
solution nmr · 1 distinct chain · 58% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chemosensory protein CSP2 | protein | 112 | 58% helix, 0% strand | Q9NG96 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 123 | 0.78 | 0.96 | 28 | empty |
| 2 | 55 | 0.42 | 0.82 | 17 | empty |
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1K19 · NMR Solution Structure of the Chemosensory Protein CSP2 from Moth Mamestra brassicae · 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 Q9NG96
- Elsewhere: RCSB PDB 1K19 · PDBe 1K19 · UniProt Q9NG96
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