2.300 Å
X-ray
2004-09-02
Name: | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 |
---|---|
ID: | AT2A1_RABIT |
AC: | P04191 |
Organism: | Oryctolagus cuniculus |
Reign: | Eukaryota |
TaxID: | 9986 |
EC Number: | 3.6.3.8 |
Chain Name: | Percentage of Residues within binding site |
---|---|
C | 100 % |
B-Factor: | 32.827 |
---|---|
Number of residues: | 25 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.262 | 725.625 |
% Hydrophobic | % Polar |
---|---|
45.12 | 54.88 |
According to VolSite |
HET Code: | ADP |
---|---|
Formula: | C10H12N5O10P2 |
Molecular weight: | 424.177 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 44.23 % |
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 |
---|---|---|
29.2114 | 75.7026 | 61.4675 |
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 |
O2B | NZ | LYS- 205 | 3.49 | 158.08 | H-Bond (Protein Donor) |
O2B | NZ | LYS- 205 | 3.49 | 0 | Ionic (Protein Cationic) |
C1' | CE2 | PHE- 487 | 3.67 | 0 | Hydrophobic |
C5' | CZ | PHE- 487 | 4.24 | 0 | Hydrophobic |
C2' | CD1 | LEU- 562 | 4.17 | 0 | Hydrophobic |
O1B | MG | MG- 1201 | 2.2 | 0 | Metal Acceptor |