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The solution structure of soybean calmodulin isoform 4 complexed with the vacuolar calcium ATPase BCA1 peptide

Analyse The solution structure of soybean calmodulin isoform 4 complexed with the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2L1W
Type: protein
Length: 174 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin; Vacuolar calcium ATPase BCA1 peptide
UniProt: Q39890
Ligands: CA
Pockets: 2 · best druggability 0.53

Structure

solution nmr · 2 distinct chains · 60% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin	protein	149	57% helix, 8% strand	Q39890
B	Vacuolar calcium ATPase BCA1 peptide	protein	25	76% helix, 0% strand	—

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · 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	62	0.53	0.87	15	empty
2	87	0.47	0.81	19	empty

Interfaces

1 interface between chains.

A–B · 1774 Å² buried · 12 hydrogen bonds · protein-protein

Compared structures

2L1W · The solution structure of soybean calmodulin isoform 4 complexed with the vacuolar… · 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 Q39890
Elsewhere: RCSB PDB 2L1W · PDBe 2L1W · UniProt Q39890

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