3.000 Å
X-ray
2006-05-31
Name: | Protein farnesyltransferase subunit beta |
---|---|
ID: | FNTB_HUMAN |
AC: | P49356 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 2.5.1.58 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 16 % |
B | 84 % |
B-Factor: | 34.739 |
---|---|
Number of residues: | 44 |
Including | |
Standard Amino Acids: | 42 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | ZN |
Ligandability | Volume (Å3) |
---|---|
0.882 | 1113.750 |
% Hydrophobic | % Polar |
---|---|
40.61 | 59.39 |
According to VolSite |
HET Code: | CYS_VAL_LEU_SER_GER |
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Formula: | C17H32N4O6S |
Molecular weight: | 420.524 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 54.52 % |
Polar Surface area: | 214.09 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 6 |
Rings: | 0 |
Aromatic rings: | 0 |
Anionic atoms: | 1 |
Cationic atoms: | 1 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 12 |
X | Y | Z |
---|---|---|
16.9799 | 132.824 | -3.49385 |
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 |
CG2 | CE1 | TYR- 166 | 4.18 | 0 | Hydrophobic |
CD1 | CZ2 | TRP- 606 | 3.81 | 0 | Hydrophobic |
CB | CB | ALA- 651 | 3.69 | 0 | Hydrophobic |
O | NH1 | ARG- 702 | 2.59 | 133.44 | H-Bond (Protein Donor) |
SG | SG | CYS- 799 | 3.95 | 0 | Hydrophobic |
CD1 | CZ2 | TRP- 803 | 4.42 | 0 | Hydrophobic |
CD2 | CZ2 | TRP- 803 | 4.33 | 0 | Hydrophobic |
CB | CE2 | TYR- 861 | 3.79 | 0 | Hydrophobic |
CD2 | CE1 | TYR- 861 | 3.58 | 0 | Hydrophobic |