MolNFT v1 · #25440 · protein

The 1.9 ångström structure of E84K-calmodulin RS20 peptide complex

1VRK: “The 1.9 ångström structure of E84K-calmodulin RS20 peptide complex”. X-ray diffraction, 2 ligands (CA, NH2), 1 pocket (best druggability 0.53). MolNFT v1 #25440 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1VRK
Type: protein
Length: 168 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Calmodulin; RS20
EC: 2.7.1.117
Ligands: CA, NH2
Pockets: 1 · best druggability 0.53

Structure

x-ray diffraction · 2 distinct chains · 62% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Calmodulin	protein	148	59% helix, 4% strand	—
B	RS20 (EC 2.7.1.117)	protein	20	80% helix, 0% strand	—

Ligands and binding sites

CA · Calcium ion · metal · 4 copies · chains A
NH2 · Amino group · ion · chains B
ACT · Acetate ion · additive · chains A, B

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	161	0.53	0.80	32	ACT

Interfaces

1 interface between chains.

A–B · 1542 Å² buried · 17 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (nonstandard).

Compared structures

1VRK · The 1.9 ångström structure of E84K-calmodulin RS20 peptide complex · 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
Elsewhere: RCSB PDB 1VRK · PDBe 1VRK

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