2.600 Å
X-ray
2008-01-30
Name: | Rhodopsin kinase |
---|---|
ID: | RK_BOVIN |
AC: | P28327 |
Organism: | Bos taurus |
Reign: | Eukaryota |
TaxID: | 9913 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 38.927 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 28 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MG MG |
Ligandability | Volume (Å3) |
---|---|
0.840 | 722.250 |
% Hydrophobic | % Polar |
---|---|
48.13 | 51.87 |
According to VolSite |
HET Code: | ADP |
---|---|
Formula: | C10H12N5O10P2 |
Molecular weight: | 424.177 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 55.38 % |
Polar Surface area: | 260.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 14 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 3 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 6 |
X | Y | Z |
---|---|---|
5.70048 | 43.697 | -22.7385 |
Represent the protein/ligand binding mode, centered on the ligand
Dashed lines represents hydrogen bonds and metal interactions
Green residue labels for amino acids with hydrophobic contacts (green lines) to the ligand
Ligand | Protein | Interaction | |||
---|---|---|---|---|---|
Atom | Atom | Residue | Distance (Å) | Angle (°) | Type |
O1B | N | GLY- 197 | 2.75 | 152.18 | H-Bond (Protein Donor) |
C1' | CB | VAL- 201 | 3.98 | 0 | Hydrophobic |
C5' | CG2 | VAL- 201 | 3.83 | 0 | Hydrophobic |
O2B | NZ | LYS- 216 | 2.86 | 142.31 | H-Bond (Protein Donor) |
O1A | NZ | LYS- 216 | 2.54 | 169.8 | H-Bond (Protein Donor) |
O2B | NZ | LYS- 216 | 2.86 | 0 | Ionic (Protein Cationic) |
O1A | NZ | LYS- 216 | 2.54 | 0 | Ionic (Protein Cationic) |
N6 | O | THR- 265 | 2.86 | 159.81 | H-Bond (Ligand Donor) |
N1 | N | MET- 267 | 3.02 | 150.23 | H-Bond (Protein Donor) |
O2A | MG | MG- 563 | 2.1 | 0 | Metal Acceptor |
O2B | MG | MG- 564 | 2.16 | 0 | Metal Acceptor |