2.190 Å
X-ray
2010-01-25
Name: | Protease |
---|---|
ID: | Q82134_9DELA |
AC: | Q82134 |
Organism: | Human T-lymphotropic virus 1 |
Reign: | Viruses |
TaxID: | 11908 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 50 % |
B | 50 % |
B-Factor: | 35.988 |
---|---|
Number of residues: | 42 |
Including | |
Standard Amino Acids: | 40 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.052 | 938.250 |
% Hydrophobic | % Polar |
---|---|
46.40 | 53.60 |
According to VolSite |
HET Code: | E15 |
---|---|
Formula: | C35H52N5O5S |
Molecular weight: | 654.883 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 62.77 % |
Polar Surface area: | 180.77 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 5 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
20.4247 | 33.6277 | 25.8218 |
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 |
CAU | CD | ARG- 10 | 3.76 | 0 | Hydrophobic |
DuAr | CZ | ARG- 10 | 3.9 | 106.41 | Pi/Cation |
CBA | CD2 | LEU- 30 | 4.43 | 0 | Hydrophobic |
CAI | CD2 | LEU- 30 | 3.53 | 0 | Hydrophobic |
OAN | OD2 | ASP- 32 | 2.84 | 146.12 | H-Bond (Protein Donor) |
OAO | OD2 | ASP- 32 | 2.94 | 121.92 | H-Bond (Protein Donor) |
OAO | OD1 | ASP- 32 | 2.75 | 162.96 | H-Bond (Ligand Donor) |
OAO | OD2 | ASP- 32 | 3.19 | 133.15 | H-Bond (Ligand Donor) |
NBC | O | GLY- 34 | 3.18 | 161.89 | H-Bond (Ligand Donor) |
CAB | CB | ALA- 35 | 4.23 | 0 | Hydrophobic |
CAC | CB | ALA- 35 | 4.04 | 0 | Hydrophobic |
CG2 | CB | ALA- 35 | 3.84 | 0 | Hydrophobic |
NAJ | OD2 | ASP- 36 | 2.68 | 161.43 | H-Bond (Ligand Donor) |
NAJ | OD2 | ASP- 36 | 2.68 | 0 | Ionic (Ligand Cationic) |
OAK | N | ASP- 36 | 3.04 | 168.91 | H-Bond (Protein Donor) |
CG2 | CG2 | VAL- 39 | 4.17 | 0 | Hydrophobic |
CBS | CG2 | VAL- 39 | 4.25 | 0 | Hydrophobic |
CG1 | CG1 | VAL- 56 | 3.52 | 0 | Hydrophobic |
CAA | CG1 | VAL- 56 | 3.2 | 0 | Hydrophobic |
N | O | LEU- 57 | 3.12 | 154.57 | H-Bond (Ligand Donor) |
CAT | CD2 | LEU- 57 | 3.71 | 0 | Hydrophobic |
CG1 | CB | ALA- 59 | 3.5 | 0 | Hydrophobic |
CAB | CB | ALA- 59 | 4.43 | 0 | Hydrophobic |
CAR | CB | ALA- 59 | 3.7 | 0 | Hydrophobic |
CAG | CD1 | LEU- 91 | 3.91 | 0 | Hydrophobic |
CAA | CD1 | LEU- 91 | 4.47 | 0 | Hydrophobic |
CAC | CD1 | LEU- 91 | 3.71 | 0 | Hydrophobic |
SBE | CZ3 | TRP- 98 | 3.92 | 0 | Hydrophobic |
CAP | CZ2 | TRP- 98 | 3.35 | 0 | Hydrophobic |
CG2 | CD1 | ILE- 100 | 4.31 | 0 | Hydrophobic |
CAR | CD1 | ILE- 100 | 4.3 | 0 | Hydrophobic |
SBE | CD1 | ILE- 100 | 4.34 | 0 | Hydrophobic |
CAB | CD1 | ILE- 100 | 4.24 | 0 | Hydrophobic |
CAV | CD1 | ILE- 100 | 3.78 | 0 | Hydrophobic |
NBB | O | HOH- 139 | 2.79 | 166.59 | H-Bond (Ligand Donor) |