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Myristoylated recoverin in the calcium-free state, NMR, 22 structures

Analyse Myristoylated recoverin in the calcium-free state, NMR, 22 structures in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1IKU
Type: protein
Length: 188 residues
Chains: 1
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Recoverin
UniProt: P21457
Ligands: MYR
Pockets: 2 · best druggability 0.78

Structure

solution nmr · 1 distinct chain · 60% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Recoverin	protein	188	60% helix, 4% strand	P21457

Ligands and binding sites

MYR · Myristic acid · ligand · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	169	0.78	0.93	29	MYR
2	79	0.38	0.77	18	empty

Modifications

Observed in the structure: 1 lipid (myristoylation).

Compared structures

1IKU · myristoylated recoverin in the calcium-free state, NMR, 22 structures · the same entry in another collection · chain A against A, TM-score 1.00
P21457 · AlphaFold monomer V2.0 prediction for recoverin (P21457) · a predicted model of the same protein · chain A against A, TM-score 0.55

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 P21457
Elsewhere: RCSB PDB 1IKU · PDBe 1IKU · UniProt P21457

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