MolNFT v1 · #179961 · protein
Structure of calmodulin bound to the cardiac ryanodine receptor (RYR2) at residues: PHE4246 to VAL4271
7KL5 · Calmodulin-1: “Structure of calmodulin bound to the cardiac ryanodine receptor (RYR2) at residues: PHE4246 to VAL4271”. X-ray diffraction, 1 ligand (CA), 3 pockets (best druggability 0.58). MolNFT v1 #179961 on GenesisL1: 3D…
- PDB
- 7KL5
- Type
- protein
- Length
- 173 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Calmodulin-1; Ryanodine receptor 2
- UniProt
- P0DP23, Q92736
- Ligands
- CA
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Calmodulin-1 | protein | 145 | 62% helix, 6% strand | P0DP23 |
| B | Ryanodine receptor 2 | protein | 28 | 93% helix, 0% strand | Q92736 |
Ligands and binding sites
- CA · Calcium ion · metal · 5 copies · chains A
- EDO · 1,2-ethanediol · additive · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 299 | 0.58 | 0.77 | 35 | empty |
| 2 | 86 | 0.43 | 0.79 | 15 | EDO |
| 3 | 70 | 0.29 | 0.72 | 17 | EDO |
Interfaces
1 interface between chains.
- A–B · 1334 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 7KL5 · Structure of Calmodulin Bound to the Cardiac Ryanodine Receptor (RyR2) at Residues… · the same entry in another collection · chain A against A, TM-score 1.00
- P0DP23 · AlphaFold monomer V2.0 prediction for calmodulin-1 (P0DP23) · a predicted model of the same protein · chain A against A, TM-score 0.54
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 P0DP23
- Every structure of UniProt Q92736
- Elsewhere: RCSB PDB 7KL5 · PDBe 7KL5 · UniProt P0DP23 · UniProt Q92736
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