Research workbench
NMR solution structure of the gs-tamapin mutation R7A
Analyse NMR solution structure of the gs-tamapin mutation R7A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MEL
- Type
- protein
- Length
- 33 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Potassium channel toxin alpha-ktx 5.4
- UniProt
- P59869
Structure
solution nmr · 1 distinct chain · 33% helix, 36% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Potassium channel toxin alpha-ktx 5.4 | protein | 33 | 33% helix, 36% strand | P59869 |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 2MEL · NMR solution structure of the GS-TAMAPIN MUTATION R7A · the same entry in another collection · chain A against A, TM-score 1.00
- P59869 · AlphaFold monomer V2.0 prediction for potassium channel toxin alpha- ktx 5.4 (P59869) · a predicted model of the same protein · chain A against A, TM-score 0.68
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 P59869
- Elsewhere: RCSB PDB 2MEL · PDBe 2MEL · UniProt P59869
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