2.750 Å
X-ray
2012-08-29
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 | 6 % |
B | 94 % |
B-Factor: | 35.694 |
---|---|
Number of residues: | 31 |
Including | |
Standard Amino Acids: | 29 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | ZN |
Ligandability | Volume (Å3) |
---|---|
0.563 | 681.750 |
% Hydrophobic | % Polar |
---|---|
43.56 | 56.44 |
According to VolSite |
HET Code: | 7TP |
---|---|
Formula: | C33H32N4O6S |
Molecular weight: | 612.695 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 47.52 % |
Polar Surface area: | 126.49 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 1 |
Rings: | 6 |
Aromatic rings: | 5 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 9 |
X | Y | Z |
---|---|---|
51.3104 | 51.7714 | -4.18725 |
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 |
CAQ | CD2 | LEU- 96 | 4.02 | 0 | Hydrophobic |
CAX | CH2 | TRP- 106 | 3.86 | 0 | Hydrophobic |
CAH | CD | ARG- 202 | 4.07 | 0 | Hydrophobic |
CAX | CD1 | TYR- 361 | 3.71 | 0 | Hydrophobic |
CAZ | CZ | TYR- 361 | 3.96 | 0 | Hydrophobic |
CAW | CE1 | TYR- 361 | 3.84 | 0 | Hydrophobic |
CAV | CB | TYR- 361 | 3.44 | 0 | Hydrophobic |
NBA | ZN | ZN- 501 | 1.98 | 0 | Metal Acceptor |
DuAr | ZN | ZN- 501 | 3.11 | 88.84 | Pi/Cation |