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Solution NMR structure of cam bound to inos cam binding domain peptide

Analyse Solution NMR structure of cam bound to inos cam binding domain peptide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2LL6
Type
protein
Length
165 residues
Chains
2
Method
solution nmr
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Calmodulin; Nitric oxide synthase, inducible
EC
1.14.13.39
UniProt
P62158, P35228
Pockets
3 · best druggability 0.64

Structure

solution nmr · 2 distinct chains · 57% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACalmodulinprotein14855% helix, 5% strandP62158
BNitric oxide synthase, inducible (EC 1.14.13.39)protein1771% helix, 0% strandP35228

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12360.640.8232empty
21110.520.8118empty
31070.430.7719empty

Interfaces

1 interface between chains.

  • A–B · 1370 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 2LL6 · Solution NMR structure of CaM bound to iNOS CaM binding domain peptide · the same entry in another collection · chain B against B, TM-score 1.00
  • P35228 · AlphaFold monomer V2.0 prediction for nitric oxide synthase, inducible (P35228) · a predicted model of the same protein · chain B against A, TM-score 0.48

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