2.700 Å
X-ray
2008-05-09
Name: | Beta-1 adrenergic receptor |
---|---|
ID: | ADRB1_MELGA |
AC: | P07700 |
Organism: | Meleagris gallopavo |
Reign: | Eukaryota |
TaxID: | 9103 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 31.972 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.021 | 452.250 |
% Hydrophobic | % Polar |
---|---|
61.19 | 38.81 |
According to VolSite |
HET Code: | P32 |
---|---|
Formula: | C16H22N3O2 |
Molecular weight: | 288.365 g/mol |
DrugBank ID: | DB08347 |
Buried Surface Area: | 69.11 % |
Polar Surface area: | 82.22 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 2 |
Rings: | 2 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 6 |
X | Y | Z |
---|---|---|
26.3763 | 5.10305 | 1.89881 |
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 |
C14 | CH2 | TRP- 117 | 3.52 | 0 | Hydrophobic |
C13 | CG2 | THR- 118 | 3.82 | 0 | Hydrophobic |
O2 | OD1 | ASP- 121 | 2.57 | 162.75 | H-Bond (Ligand Donor) |
O2 | OD2 | ASP- 121 | 3.11 | 120.38 | H-Bond (Ligand Donor) |
N2 | OD2 | ASP- 121 | 2.95 | 149.43 | H-Bond (Ligand Donor) |
N2 | OD2 | ASP- 121 | 2.95 | 0 | Ionic (Ligand Cationic) |
C13 | CB | ASP- 121 | 4.44 | 0 | Hydrophobic |
C9 | CG2 | VAL- 122 | 4.18 | 0 | Hydrophobic |
C4 | CG2 | VAL- 122 | 3.92 | 0 | Hydrophobic |
C6 | CG1 | VAL- 122 | 3.41 | 0 | Hydrophobic |
C9 | CG2 | VAL- 125 | 4.13 | 0 | Hydrophobic |
C5 | CB | VAL- 125 | 4.41 | 0 | Hydrophobic |
C15 | CB | PHE- 201 | 3.74 | 0 | Hydrophobic |
C13 | CD2 | PHE- 201 | 4.27 | 0 | Hydrophobic |
N1 | OG | SER- 211 | 2.81 | 163.98 | H-Bond (Ligand Donor) |
C7 | CB | SER- 215 | 3.72 | 0 | Hydrophobic |
C10 | CZ3 | TRP- 303 | 4.33 | 0 | Hydrophobic |
C10 | CZ | PHE- 306 | 3.82 | 0 | Hydrophobic |
C9 | CE2 | PHE- 306 | 4.21 | 0 | Hydrophobic |
N3 | ND2 | ASN- 310 | 3.3 | 164.24 | H-Bond (Protein Donor) |
O2 | ND2 | ASN- 329 | 3.03 | 144.66 | H-Bond (Protein Donor) |
N2 | OD1 | ASN- 329 | 2.61 | 149.11 | H-Bond (Ligand Donor) |