2.000 Å
X-ray
2008-11-04
Name: | Ras-related C3 botulinum toxin substrate 2 |
---|---|
ID: | RAC2_HUMAN |
AC: | P15153 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
D | 100 % |
B-Factor: | 26.590 |
---|---|
Number of residues: | 36 |
Including | |
Standard Amino Acids: | 34 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.080 | 263.250 |
% Hydrophobic | % Polar |
---|---|
43.59 | 56.41 |
According to VolSite |
HET Code: | GTP |
---|---|
Formula: | C10H12N5O14P3 |
Molecular weight: | 519.149 g/mol |
DrugBank ID: | DB04137 |
Buried Surface Area: | 65.45 % |
Polar Surface area: | 335.56 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
15.2186 | 58.8607 | 30.0266 |
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 | ALA- 13 | 2.74 | 135.27 | H-Bond (Protein Donor) |
O2B | N | ALA- 13 | 3.04 | 137.81 | H-Bond (Protein Donor) |
C5' | CB | ALA- 13 | 4.31 | 0 | Hydrophobic |
O2B | N | VAL- 14 | 3.3 | 135.38 | H-Bond (Protein Donor) |
O2B | N | GLY- 15 | 3.42 | 153.22 | H-Bond (Protein Donor) |
O3A | N | GLY- 15 | 2.78 | 121.71 | H-Bond (Protein Donor) |
O2G | NZ | LYS- 16 | 3.92 | 0 | Ionic (Protein Cationic) |
O3G | NZ | LYS- 16 | 3.81 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 16 | 2.68 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 16 | 2.68 | 144.06 | H-Bond (Protein Donor) |
O2B | N | LYS- 16 | 3.42 | 161.22 | H-Bond (Protein Donor) |
O3B | N | THR- 17 | 3.26 | 155.06 | H-Bond (Protein Donor) |
O1A | N | CYS- 18 | 2.78 | 174.88 | H-Bond (Protein Donor) |
C2' | SG | CYS- 18 | 4.1 | 0 | Hydrophobic |
C2' | CZ | PHE- 28 | 4.21 | 0 | Hydrophobic |
C3' | CD1 | ILE- 33 | 3.34 | 0 | Hydrophobic |
O4' | NZ | LYS- 116 | 2.89 | 141.63 | H-Bond (Protein Donor) |
N1 | OD1 | ASP- 118 | 2.77 | 148.75 | H-Bond (Ligand Donor) |
N1 | OD2 | ASP- 118 | 3.35 | 130.26 | H-Bond (Ligand Donor) |
N2 | OD2 | ASP- 118 | 2.75 | 168.01 | H-Bond (Ligand Donor) |
O6 | OG | SER- 158 | 3.3 | 178.05 | H-Bond (Protein Donor) |
O6 | N | ALA- 159 | 2.73 | 121.79 | H-Bond (Protein Donor) |
O6 | N | LEU- 160 | 3.17 | 157.75 | H-Bond (Protein Donor) |
O3G | O | HOH- 2110 | 2.62 | 164.61 | H-Bond (Protein Donor) |