Research workbench
Solution structure of calmodulin bound to the target peptide of endothelial nitrogen oxide synthase phosphorylated at THR495
Analyse Solution structure of calmodulin bound to the target peptide of endothelial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MG5
- Type
- protein
- Length
- 164 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin; Target peptide
- UniProt
- P62158
- Pockets
- 1 · best druggability 0.41
Structure
solution nmr · 2 distinct chains · 46% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin | protein | 148 | 46% helix, 0% strand | P62158 |
| B | Target peptide | protein | 16 | 44% helix, 0% strand | — |
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 | 91 | 0.41 | 0.77 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 1363 Ų buried · 9 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 modified (phosphorylation).
Compared structures
- 2MG5 · Solution Structure of Calmodulin bound to the target peptide of Endothelial Nitrogen… · the same entry in another collection · chain A against A, TM-score 1.00
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 P62158
- Elsewhere: RCSB PDB 2MG5 · PDBe 2MG5 · UniProt P62158
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