GL1X · GenesisL1 explorer

MolNFT v1 · #180716 · protein

NMR structure of half-calcified calmodulin mutant (CAMEF12) bound to the iq-motif of CAV1.2

7L8V · Calmodulin-1: “NMR structure of half-calcified calmodulin mutant (CAMEF12) bound to the iq-motif of CAV1.2”. Solution nmr, 1 ligand (CA), 3 pockets (best druggability 0.74). MolNFT v1 #180716 on GenesisL1: 3D structure, binding…

PDB
7L8V
Type
protein
Length
170 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Calmodulin-1; Voltage-dependent L-type calcium channel subunit alpha-1C
UniProt
P0DP23, Q13936
Ligands
CA
Pockets
3 · best druggability 0.74

Structure

solution nmr · 2 distinct chains · 56% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACalmodulin-1protein14954% helix, 5% strandP0DP23
CVoltage-dependent L-type calcium channel subunit alpha-1Cprotein2167% helix, 0% strandQ13936

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

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1910.740.9515empty
21220.580.8420empty
3690.400.7921empty

Interfaces

1 interface between chains.

  • A–C · 777 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7L8V · NMR Structure of half-calcified calmodulin mutant (CaMEF12) bound to the IQ-motif of… · 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 0.47
  • Q13936 · AlphaFold monomer V2.0 prediction for voltage-dependent L-type calcium channel subunit… · a predicted model of the same protein · chain C against A, TM-score 0.45

Analyse

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.