2.300 Å
X-ray
2004-10-01
Min | Mean | Median | Standard Deviation | Max | Count | |
---|---|---|---|---|---|---|
pChEMBL: | 8.520 | 8.520 | 8.520 | 0.000 | 8.520 | 1 |
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 |
---|---|
A | 100 % |
B-Factor: | 27.733 |
---|---|
Number of residues: | 38 |
Including | |
Standard Amino Acids: | 38 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.489 | 739.125 |
% Hydrophobic | % Polar |
---|---|
38.36 | 61.64 |
According to VolSite |
HET Code: | GAH |
---|---|
Formula: | C38H63N11O6 |
Molecular weight: | 769.977 g/mol |
DrugBank ID: | DB04697 |
Buried Surface Area: | 50.26 % |
Polar Surface area: | 298.2 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 10 |
H-Bond Donors: | 11 |
Rings: | 4 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 2 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 21 |
X | Y | Z |
---|---|---|
12.837 | -14.7946 | 14.0839 |
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 |
C27 | CB | HIS- 57 | 4.34 | 0 | Hydrophobic |
C27 | CZ | TYR- 60 | 4.35 | 0 | Hydrophobic |
C27 | CH2 | TRP- 60 | 4 | 0 | Hydrophobic |
C51 | CH2 | TRP- 60 | 3.64 | 0 | Hydrophobic |
C20 | CB | ASN- 98 | 4.37 | 0 | Hydrophobic |
C19 | CD2 | LEU- 99 | 4.32 | 0 | Hydrophobic |
C27 | CD2 | LEU- 99 | 3.62 | 0 | Hydrophobic |
C20 | CD1 | LEU- 99 | 4.23 | 0 | Hydrophobic |
C22 | CD1 | ILE- 174 | 4.48 | 0 | Hydrophobic |
C20 | CD1 | ILE- 174 | 4.12 | 0 | Hydrophobic |
C18 | CD1 | ILE- 174 | 3.55 | 0 | Hydrophobic |
O40 | OD1 | ASP- 189 | 3.36 | 171.32 | H-Bond (Ligand Donor) |
C38 | CB | ALA- 190 | 3.65 | 0 | Hydrophobic |
C49 | CG | GLU- 192 | 4.47 | 0 | Hydrophobic |
C33 | CB | SER- 195 | 3.38 | 0 | Hydrophobic |
C34 | CG1 | VAL- 213 | 3.77 | 0 | Hydrophobic |
C35 | CG1 | VAL- 213 | 3.3 | 0 | Hydrophobic |
N31 | O | SER- 214 | 3.36 | 143.84 | H-Bond (Ligand Donor) |
C19 | CD2 | TRP- 215 | 3.62 | 0 | Hydrophobic |
C16 | CE3 | TRP- 215 | 3.62 | 0 | Hydrophobic |
O24 | N | GLY- 216 | 3.39 | 172.79 | H-Bond (Protein Donor) |
C1 | CB | GLU- 217 | 3.85 | 0 | Hydrophobic |
O46 | N | GLY- 219 | 2.76 | 157.08 | H-Bond (Protein Donor) |
N47 | O | GLY- 219 | 2.95 | 126.73 | H-Bond (Ligand Donor) |