1.770 Å
X-ray
2013-07-14
Name: | Prothrombin |
---|---|
ID: | THRB_HUMAN |
AC: | P00734 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 3.4.21.5 |
Chain Name: | Percentage of Residues within binding site |
---|---|
H | 100 % |
B-Factor: | 24.554 |
---|---|
Number of residues: | 34 |
Including | |
Standard Amino Acids: | 34 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.277 | 381.375 |
% Hydrophobic | % Polar |
---|---|
38.05 | 61.95 |
According to VolSite |
HET Code: | 6XS |
---|---|
Formula: | C24H29Cl2FN5O5S2 |
Molecular weight: | 621.552 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 62.27 % |
Polar Surface area: | 156.94 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 3 |
Rings: | 4 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
11.9868 | -13.9906 | 13.6625 |
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 |
F13 | CE2 | TYR- 60 | 3.84 | 0 | Hydrophobic |
F13 | CZ2 | TRP- 60 | 3.43 | 0 | Hydrophobic |
C1 | CG | LEU- 99 | 3.76 | 0 | Hydrophobic |
C6 | CG2 | ILE- 174 | 4 | 0 | Hydrophobic |
C5 | CD1 | ILE- 174 | 3.68 | 0 | Hydrophobic |
CL3 | CB | ALA- 190 | 3.91 | 0 | Hydrophobic |
S30 | CB | ALA- 190 | 4.15 | 0 | Hydrophobic |
CL3 | CG1 | VAL- 213 | 3.65 | 0 | Hydrophobic |
S30 | CG1 | VAL- 213 | 3.49 | 0 | Hydrophobic |
CL4 | CE3 | TRP- 215 | 3.78 | 0 | Hydrophobic |
C1 | CD2 | TRP- 215 | 3.7 | 0 | Hydrophobic |
O38 | N | GLY- 216 | 3.12 | 164.26 | H-Bond (Protein Donor) |
N16 | O | GLY- 216 | 2.83 | 140.27 | H-Bond (Ligand Donor) |
CL4 | CG | GLU- 217 | 4.11 | 0 | Hydrophobic |
N27 | O | GLY- 219 | 3.23 | 169.91 | H-Bond (Ligand Donor) |
O36 | N | GLY- 219 | 3.22 | 153.5 | H-Bond (Protein Donor) |
CL3 | CZ | TYR- 228 | 3.62 | 0 | Hydrophobic |