Research workbench
Site III-site IV troponin C heterodimer, NMR
Analyse Site III-site IV troponin C heterodimer, NMR in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1PON
- Type
- protein
- Length
- 68 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Troponin C
- UniProt
- P02588
- Ligands
- ACE, NH2
- Pockets
- 1 · best druggability 0.38
Structure
solution nmr · 2 distinct chains · 54% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Troponin C | protein | 34 | 50% helix, 6% strand | P02588 |
| B | Troponin C | protein | 34 | 59% helix, 6% strand | P02588 |
Ligands and binding sites
- ACE · Acetyl group · ligand · 2 copies · chains A, B
- NH2 · Amino group · ion · 2 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 | 66 | 0.38 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 628 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 covalent (covalent ligand).
Compared structures
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 1PON · PDBe 1PON · UniProt P02588
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.