MolNFT v1 · #13324 · protein

Crystal structure of CA2+/CALMODULIN complexed with myristoylated cap-23/NAP-22 peptide

1L7Z: “Crystal structure of CA2+/CALMODULIN complexed with myristoylated cap-23/NAP-22 peptide”. X-ray diffraction, 2 ligands (MYR, CA), 1 pocket (best druggability 0.79). MolNFT v1 #13324 on GenesisL1: 3D structure, binding sites and…

PDB: 1L7Z
Type: protein
Length: 148 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin; Cap-23/NAP-22
UniProt: P62158
Ligands: MYR, CA
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 53% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin	protein	142	55% helix, 6% strand	P62158
B	Cap-23/NAP-22	protein	6	0% helix, 0% strand	—

Ligands and binding sites

MYR · Myristic acid · ligand · chains A, B
CA · Calcium ion · metal · 4 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1005	0.79	0.80	58	MYR

Interfaces

1 interface between chains.

A–B · 392 Å² buried · 2 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 lipid (myristoylation).

Compared structures

1L7Z · Crystal structure of Ca2+/Calmodulin complexed with myristoylated CAP-23/NAP-22 peptide · the same entry in another collection · chain B against B, 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
Elsewhere: RCSB PDB 1L7Z · PDBe 1L7Z · UniProt P62158

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