Research workbench
X-ray crystallographic study of calcium-saturated N- terminal domain of troponin C
Analyse X-ray crystallographic study of calcium-saturated N- terminal domain of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1AVS
- Type
- protein
- Length
- 163 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Troponin C
- UniProt
- P02588
- Ligands
- CA
- Pockets
- 1 · best druggability 0.41
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Troponin C | protein | 81 | 63% helix, 6% strand | P02588 |
| B | Troponin C | protein | 82 | 62% helix, 6% strand | P02588 |
Ligands and binding sites
- CA · Calcium ion · metal · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 75 | 0.41 | 0.79 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 378 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1AVS · X-ray crystallographic study of calcium-saturated N-terminal domain of troponin C · the same entry in another collection · chain A against A, TM-score 1.00
- P02588 · AlphaFold monomer V2.0 prediction for troponin C, skeletal muscle (P02588) · a predicted model of the same protein · chain B against A, TM-score 0.93
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 P02588
- Elsewhere: RCSB PDB 1AVS · PDBe 1AVS · UniProt P02588
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