Research workbench
Structure of a rhodamine-labeled N-domain troponin C mutant (CA2+ saturated) in complex with skeletal troponin I 115-131
Analyse Structure of a rhodamine-labeled N-domain troponin C mutant (CA2+ saturated) in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NPQ
- Type
- protein
- Length
- 107 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Troponin C; Troponin I
- UniProt
- P02588, P02643
- Ligands
- CA
- Pockets
- 2 · best druggability 0.59
Structure
solution nmr · 2 distinct chains · 52% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Troponin C | protein | 90 | 54% helix, 2% strand | P02588 |
| B | Troponin I | protein | 17 | 41% 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 | 54 | 0.59 | 0.91 | 20 | empty |
| 2 | 50 | 0.36 | 0.79 | 9 | empty |
Interfaces
1 interface between chains.
- A–B · 745 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 1NPQ · structure of a rhodamine-labeled N-domain Troponin C mutant (Ca2+ saturated) in complex… · 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 A against A, TM-score 0.71
- 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 0.30
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
- Every structure of UniProt P02643
- Elsewhere: RCSB PDB 1NPQ · PDBe 1NPQ · UniProt P02588 · UniProt P02643
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