2.000 Å
X-ray
2002-10-07
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 | 20 % |
B | 80 % |
B-Factor: | 14.995 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 28 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | ZN |
Ligandability | Volume (Å3) |
---|---|
0.658 | 1015.875 |
% Hydrophobic | % Polar |
---|---|
35.55 | 64.45 |
According to VolSite |
HET Code: | BNE |
---|---|
Formula: | C28H34N5O2 |
Molecular weight: | 472.602 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 58.56 % |
Polar Surface area: | 98.79 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 1 |
Rings: | 4 |
Aromatic rings: | 3 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 6 |
X | Y | Z |
---|---|---|
17.1398 | 133.836 | -2.6392 |
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 |
C5 | CD2 | LEU- 596 | 3.8 | 0 | Hydrophobic |
C4 | CB | SER- 599 | 4.07 | 0 | Hydrophobic |
C13 | CZ3 | TRP- 602 | 3.48 | 0 | Hydrophobic |
C10 | CE2 | TRP- 602 | 3.93 | 0 | Hydrophobic |
C11 | CH2 | TRP- 606 | 3.35 | 0 | Hydrophobic |
C10 | CB | ALA- 651 | 3.64 | 0 | Hydrophobic |
N26 | NH1 | ARG- 702 | 2.92 | 127.92 | H-Bond (Protein Donor) |
C11 | CD1 | TYR- 861 | 4.5 | 0 | Hydrophobic |
NZ | ZN | ZN- 1001 | 1.93 | 0 | Metal Acceptor |
DuAr | ZN | ZN- 1001 | 3.11 | 83.52 | Pi/Cation |