Research workbench
NMR structure of the dilated cardiomyopathy mutation G159D in troponin C bound to the anchoring region of troponin I
Analyse NMR structure of the dilated cardiomyopathy mutation G159D in troponin C bound… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MLF
- Type
- protein
- Length
- 72 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P63316
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | — | protein | 72 | — | P63316 |
Compared structures
- 2MLF · NMR structure of the dilated cardiomyopathy mutation G159D in troponin C bound to the… · the same entry in another collection · chain C against C, TM-score 1.00
- P63316 · AlphaFold monomer V2.0 prediction for troponin C, slow skeletal and cardiac muscles… · a predicted model of the same protein · chain C against A, TM-score 0.65
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 P63316
- Elsewhere: RCSB PDB 2MLF · PDBe 2MLF · UniProt P63316
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