2.100 Å
X-ray
2010-12-14
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 | 12 % |
B | 88 % |
B-Factor: | 23.832 |
---|---|
Number of residues: | 25 |
Including | |
Standard Amino Acids: | 23 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | ZN |
Ligandability | Volume (Å3) |
---|---|
0.834 | 1326.375 |
% Hydrophobic | % Polar |
---|---|
39.69 | 60.31 |
According to VolSite |
HET Code: | 3PZ |
---|---|
Formula: | C29H29N5O3S |
Molecular weight: | 527.637 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 47.41 % |
Polar Surface area: | 99.83 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 0 |
Rings: | 5 |
Aromatic rings: | 4 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
51.0665 | -50.9943 | 4.20639 |
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 |
N3 | ZN | ZN- 1 | 2.13 | 0 | Metal Acceptor |
DuAr | ZN | ZN- 1 | 3.21 | 92.28 | Pi/Cation |
C23 | SG | CYS- 95 | 3.88 | 0 | Hydrophobic |
C7 | CD2 | LEU- 96 | 4.49 | 0 | Hydrophobic |
C24 | CD2 | LEU- 96 | 4.06 | 0 | Hydrophobic |
C3 | CD1 | LEU- 96 | 4.04 | 0 | Hydrophobic |
C7 | CH2 | TRP- 106 | 3.96 | 0 | Hydrophobic |
C7 | CD1 | TYR- 361 | 4.14 | 0 | Hydrophobic |
C9 | CZ | TYR- 361 | 4.23 | 0 | Hydrophobic |
C4 | CB | TYR- 361 | 3.2 | 0 | Hydrophobic |