GL1X · GenesisL1 explorer

Research workbench

Structure and 15N relaxation data of calmodulin bound to the endothelial nitric oxide synthase calmodulin binding domain peptide at physiological calcium concentration

Analyse Structure and 15N relaxation data of calmodulin bound to the endothelial nitric… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2N8J
Type
protein
Length
170 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Calmodulin; Nitric oxide synthase, endothelial
UniProt
P62158, P29474
Pockets
2 · best druggability 0.49

Structure

solution nmr · 2 distinct chains · 36% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACalmodulinprotein14837% helix, 5% strandP62158
BNitric oxide synthase, endothelialprotein2232% helix, 0% strandP29474

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11560.490.7830empty
2650.300.7413empty

Interfaces

1 interface between chains.

  • A–B · 1208 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 2N8J · Structure and 15N relaxation data of Calmodulin bound to the endothelial Nitric Oxide… · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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