2.100 Å
X-ray
2009-11-23
Name: | Protein farnesyltransferase subunit beta |
---|---|
ID: | FNTB_RAT |
AC: | Q02293 |
Organism: | Rattus norvegicus |
Reign: | Eukaryota |
TaxID: | 10116 |
EC Number: | 2.5.1.58 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 19 % |
B | 81 % |
B-Factor: | 35.641 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 29 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | ZN |
Ligandability | Volume (Å3) |
---|---|
0.586 | 901.125 |
% Hydrophobic | % Polar |
---|---|
41.20 | 58.80 |
According to VolSite |
HET Code: | Z96 |
---|---|
Formula: | C28H33ClN5O3 |
Molecular weight: | 523.046 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 50.21 % |
Polar Surface area: | 84.92 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 2 |
Rings: | 5 |
Aromatic rings: | 3 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 5 |
X | Y | Z |
---|---|---|
187.365 | 129.559 | 33.5458 |
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 |
C22 | CZ | TYR- 93 | 4.33 | 0 | Hydrophobic |
C26 | CE2 | TYR- 93 | 3.71 | 0 | Hydrophobic |
C26 | SG | CYS- 95 | 3.62 | 0 | Hydrophobic |
C24 | SG | CYS- 95 | 3.96 | 0 | Hydrophobic |
C26 | CD1 | LEU- 96 | 3.82 | 0 | Hydrophobic |
CL | CB | LYS- 164 | 4.32 | 0 | Hydrophobic |
CL | CD1 | TYR- 166 | 4 | 0 | Hydrophobic |
C22 | CB | ASP- 359 | 3.67 | 0 | Hydrophobic |
C4 | CE1 | TYR- 361 | 3.28 | 0 | Hydrophobic |
N3 | ZN | ZN- 2001 | 2.14 | 0 | Metal Acceptor |
DuAr | ZN | ZN- 2001 | 3.25 | 82.35 | Pi/Cation |