Research workbench
Complex of troponin C with a 47 residue (1-47) fragment of troponin I
Analyse Complex of troponin C with a 47 residue (1-47) fragment of troponin I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1A2X
- Type
- protein
- Length
- 189 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Troponin C; Troponin I
- UniProt
- P02586, P02643
- Ligands
- CA
- Pockets
- 2 · best druggability 0.65
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Troponin C | protein | 158 | 59% helix, 8% strand | P02586 |
| B | Troponin I | protein | 31 | 87% helix, 0% strand | P02643 |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 310 | 0.65 | 0.81 | 33 | empty |
| 2 | 67 | 0.30 | 0.74 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1212 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1A2X · Complex of troponin C with a 47 residue (1-47) fragment of troponin I · the same entry in another collection · chain A against A, TM-score 1.00
- P02643 · AlphaFold monomer V2.0 prediction for troponin I, fast skeletal muscle (P02643) · a predicted model of the same protein · chain B against A, TM-score 0.86
- P02586 · AlphaFold monomer V2.0 prediction for troponin C, skeletal muscle (P02586) · a predicted model of the same protein · chain A against A, TM-score 0.43
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 P02586
- Every structure of UniProt P02643
- Elsewhere: RCSB PDB 1A2X · PDBe 1A2X · UniProt P02586 · UniProt P02643
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