sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.500 Å
X-ray
2009-06-08
| Name: | Nitric oxide synthase, inducible |
|---|---|
| ID: | NOS2_HUMAN |
| AC: | P35228 |
| Organism: | Homo sapiens |
| Reign: | Eukaryota |
| TaxID: | 9606 |
| EC Number: | 1.14.13.39 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 75 % |
| C | 25 % |
| B-Factor: | 61.115 |
|---|---|
| Number of residues: | 41 |
| Including | |
| Standard Amino Acids: | 40 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 1 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 0.471 | 816.750 |
| % Hydrophobic | % Polar |
|---|---|
| 42.98 | 57.02 |
| According to VolSite | |
| HET Code: | FMN |
|---|---|
| Formula: | C17H19N4O9P |
| Molecular weight: | 454.328 g/mol |
| DrugBank ID: | DB03247 |
| Buried Surface Area: | 82.93 % |
| 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 |
|---|---|---|
| 0.989387 | 8.93539 | -65.4367 |
Image generated by PoseView
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 | OG1 | THR- 545 | 2.74 | 153.07 | H-Bond (Protein Donor) |
| O2P | N | GLU- 546 | 2.58 | 149.44 | H-Bond (Protein Donor) |
| O2P | N | THR- 547 | 2.95 | 155.2 | H-Bond (Protein Donor) |
| O4' | NZ | LYS- 549 | 2.84 | 153.27 | H-Bond (Protein Donor) |
| O3P | N | LYS- 549 | 2.67 | 158.73 | H-Bond (Protein Donor) |
| C5' | CD | LYS- 549 | 4.03 | 0 | Hydrophobic |
| O1P | N | SER- 550 | 2.92 | 133.04 | H-Bond (Protein Donor) |
| O1P | OG | SER- 550 | 2.74 | 152.48 | H-Bond (Protein Donor) |
| C2' | CB | SER- 591 | 4.44 | 0 | Hydrophobic |
| C5' | CB | SER- 591 | 3.88 | 0 | Hydrophobic |
| O5' | OG | SER- 591 | 3.31 | 126.96 | H-Bond (Protein Donor) |
| O1P | OG | SER- 591 | 3.23 | 139.81 | H-Bond (Protein Donor) |
| O2P | OG | SER- 591 | 2.85 | 154.49 | H-Bond (Protein Donor) |
| O2' | O | THR- 592 | 2.87 | 174.02 | H-Bond (Ligand Donor) |
| C8M | CE2 | PHE- 593 | 3.93 | 0 | Hydrophobic |
| C2' | CZ | PHE- 593 | 4.1 | 0 | Hydrophobic |
| C5' | CZ | PHE- 593 | 3.94 | 0 | Hydrophobic |
| C8M | CB | ASN- 595 | 4.39 | 0 | Hydrophobic |
| C7M | CB | ASP- 597 | 3.78 | 0 | Hydrophobic |
| C8M | CB | ASP- 597 | 4.08 | 0 | Hydrophobic |
| C4' | CB | LEU- 626 | 4.25 | 0 | Hydrophobic |
| O2 | N | SER- 628 | 3.22 | 151.8 | H-Bond (Protein Donor) |
| C1' | CB | SER- 628 | 3.76 | 0 | Hydrophobic |
| C1' | CE2 | TYR- 631 | 4.27 | 0 | Hydrophobic |
| N3 | O | ARG- 633 | 2.84 | 175.84 | H-Bond (Ligand Donor) |
| O2 | N | CYS- 635 | 2.73 | 177.02 | H-Bond (Protein Donor) |
| O3' | OE2 | GLU- 661 | 2.94 | 150.74 | H-Bond (Ligand Donor) |
| O4' | NE2 | GLN- 665 | 3.37 | 175.94 | H-Bond (Protein Donor) |
