2.610 Å
X-ray
2009-03-03
Name: | Iodotyrosine deiodinase 1 |
---|---|
ID: | IYD1_MOUSE |
AC: | Q9DCX8 |
Organism: | Mus musculus |
Reign: | Eukaryota |
TaxID: | 10090 |
EC Number: | 1.21.1.1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
G | 36 % |
H | 64 % |
B-Factor: | 31.319 |
---|---|
Number of residues: | 39 |
Including | |
Standard Amino Acids: | 38 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.103 | 378.000 |
% Hydrophobic | % Polar |
---|---|
40.18 | 59.82 |
According to VolSite |
HET Code: | FMN |
---|---|
Formula: | C17H19N4O9P |
Molecular weight: | 454.328 g/mol |
DrugBank ID: | DB03247 |
Buried Surface Area: | 81.38 % |
Polar Surface area: | 217.05 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 12 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
-14.1969 | -56.9993 | 39.0578 |
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 |
O2P | CZ | ARG- 96 | 3.28 | 0 | Ionic (Protein Cationic) |
O2P | NH2 | ARG- 96 | 3.12 | 129.68 | H-Bond (Protein Donor) |
O2P | NH1 | ARG- 96 | 2.6 | 157.13 | H-Bond (Protein Donor) |
O3P | NH2 | ARG- 96 | 3.38 | 131.49 | H-Bond (Protein Donor) |
O1P | CZ | ARG- 97 | 3.71 | 0 | Ionic (Protein Cationic) |
O1P | NE | ARG- 97 | 2.84 | 156.76 | H-Bond (Protein Donor) |
C1' | CB | SER- 98 | 4.44 | 0 | Hydrophobic |
C3' | CB | SER- 98 | 4.25 | 0 | Hydrophobic |
O1P | N | SER- 98 | 2.52 | 167.09 | H-Bond (Protein Donor) |
O2P | N | SER- 98 | 3.45 | 131.15 | H-Bond (Protein Donor) |
N1 | NH2 | ARG- 100 | 2.94 | 160.9 | H-Bond (Protein Donor) |
O2 | NE | ARG- 100 | 2.62 | 139.65 | H-Bond (Protein Donor) |
C8M | CB | PRO- 123 | 3.75 | 0 | Hydrophobic |
C9 | CB | PRO- 123 | 4.28 | 0 | Hydrophobic |
C3' | CB | PRO- 123 | 4.22 | 0 | Hydrophobic |
O3' | N | SER- 124 | 3.27 | 145.57 | H-Bond (Protein Donor) |
O2' | N | ALA- 126 | 3.48 | 143.8 | H-Bond (Protein Donor) |
C4' | CB | HIS- 127 | 3.82 | 0 | Hydrophobic |
C7M | CB | TYR- 208 | 3.6 | 0 | Hydrophobic |
C7M | CG2 | ILE- 211 | 3.73 | 0 | Hydrophobic |
C8M | CB | SER- 212 | 4.33 | 0 | Hydrophobic |
C8M | CD1 | ILE- 215 | 3.87 | 0 | Hydrophobic |
C1' | CG2 | VAL- 232 | 4.2 | 0 | Hydrophobic |
C8M | CG2 | THR- 233 | 4.04 | 0 | Hydrophobic |
C9 | CB | THR- 233 | 4.06 | 0 | Hydrophobic |
O4 | N | THR- 235 | 3.07 | 141.66 | H-Bond (Protein Donor) |
N5 | OG1 | THR- 235 | 3.18 | 144.9 | H-Bond (Protein Donor) |
N5 | N | THR- 235 | 3.4 | 147.76 | H-Bond (Protein Donor) |
C6 | CG2 | THR- 235 | 4.02 | 0 | Hydrophobic |
C7M | CG2 | THR- 235 | 4.42 | 0 | Hydrophobic |
C5' | CD1 | LEU- 273 | 4.05 | 0 | Hydrophobic |
O3P | NH2 | ARG- 275 | 3.42 | 157.06 | H-Bond (Protein Donor) |
N3 | O | TYI- 302 | 2.71 | 158.66 | H-Bond (Ligand Donor) |
O4 | N | TYI- 302 | 2.82 | 142.97 | H-Bond (Protein Donor) |
O2' | OH | TYI- 302 | 3.09 | 139.98 | H-Bond (Protein Donor) |
C6 | I2 | TYI- 302 | 4.26 | 0 | Hydrophobic |