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Solution NMR structure of cam bound to the enos cam binding domain peptide

Analyse Solution NMR structure of cam bound to the enos 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: 2LL7
Type: protein
Length: 165 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin; Nitric oxide synthase, endothelial
EC: 1.14.13.39
UniProt: P62158, P29474
Pockets: 2 · best druggability 0.73

Structure

solution nmr · 2 distinct chains · 47% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin	protein	148	46% helix, 4% strand	P62158
B	Nitric oxide synthase, endothelial (EC 1.14.13.39)	protein	17	53% helix, 0% strand	P29474

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	114	0.73	0.93	27	empty
2	103	0.51	0.82	26	empty

Interfaces

1 interface between chains.

A–B · 1276 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

2LL7 · Solution NMR structure of CaM bound to the eNOS CaM binding domain peptide · 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
Every structure of UniProt P29474
Elsewhere: RCSB PDB 2LL7 · PDBe 2LL7 · UniProt P62158 · UniProt P29474

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