2.300 Å
X-ray
1997-09-25
Name: | Bis(5'-adenosyl)-triphosphatase |
---|---|
ID: | FHIT_HUMAN |
AC: | P49789 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 3.6.1.29 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 30.645 |
---|---|
Number of residues: | 27 |
Including | |
Standard Amino Acids: | 27 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.690 | 442.125 |
% Hydrophobic | % Polar |
---|---|
51.91 | 48.09 |
According to VolSite |
HET Code: | AP2 |
---|---|
Formula: | C11H14N5O9P2 |
Molecular weight: | 422.204 g/mol |
DrugBank ID: | DB03148 |
Buried Surface Area: | 58.16 % |
Polar Surface area: | 251.48 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 13 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 3 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 6 |
X | Y | Z |
---|---|---|
8.31248 | 21.6181 | 24.7723 |
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 |
O3' | ND2 | ASN- 27 | 2.74 | 132.13 | H-Bond (Protein Donor) |
C4' | CD1 | LEU- 37 | 4.14 | 0 | Hydrophobic |
C1' | CD1 | LEU- 37 | 3.86 | 0 | Hydrophobic |
O1A | NE2 | GLN- 83 | 2.54 | 143.34 | H-Bond (Protein Donor) |
C3A | CG2 | THR- 91 | 4 | 0 | Hydrophobic |
O2A | N | THR- 91 | 3.16 | 145.4 | H-Bond (Protein Donor) |
O2A | N | VAL- 92 | 3.32 | 143.5 | H-Bond (Protein Donor) |
C5' | CG1 | VAL- 92 | 3.76 | 0 | Hydrophobic |
O5' | NE2 | HIS- 96 | 2.81 | 168.62 | H-Bond (Protein Donor) |
O1A | NE2 | HIS- 98 | 2.91 | 164.62 | H-Bond (Protein Donor) |