sc-PDB
An Annotated Database of Druggable Binding Sites from the Protein DataBank
An Annotated Database of Druggable Binding Sites from the Protein DataBank
2.000 Å
X-ray
2005-12-25
| Name: | Formylmethanofuran--tetrahydromethanopterin formyltransferase |
|---|---|
| ID: | FTR_METKA |
| AC: | Q49610 |
| Organism: | Methanopyrus kandleri |
| Reign: | Archaea |
| TaxID: | 190192 |
| EC Number: | 2.3.1.101 |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| C | 42 % |
| D | 58 % |
| B-Factor: | 29.368 |
|---|---|
| Number of residues: | 33 |
| Including | |
| Standard Amino Acids: | 33 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.417 | 1154.250 |
| % Hydrophobic | % Polar |
|---|---|
| 54.09 | 45.91 |
| According to VolSite | |
| HET Code: | MFN |
|---|---|
| Formula: | C35H39N4O16 |
| Molecular weight: | 771.701 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 55.12 % |
| Polar Surface area: | 339.41 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 15 |
| H-Bond Donors: | 4 |
| Rings: | 2 |
| Aromatic rings: | 2 |
| Anionic atoms: | 5 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 2 |
| Rotatable Bonds: | 27 |
| X | Y | Z |
|---|---|---|
| -4.11372 | 91.5666 | 90.9725 |
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 |
| C8 | CG2 | ILE- 48 | 4.02 | 0 | Hydrophobic |
| C11 | CE | MET- 49 | 3.47 | 0 | Hydrophobic |
| C6 | SD | MET- 49 | 3.9 | 0 | Hydrophobic |
| C18 | CD2 | LEU- 90 | 4.15 | 0 | Hydrophobic |
| C13 | CE | MET- 98 | 4.07 | 0 | Hydrophobic |
| C10 | CE | MET- 98 | 3.23 | 0 | Hydrophobic |
| C13 | CG2 | THR- 99 | 4.28 | 0 | Hydrophobic |
| C22 | CG | LYS- 123 | 4.48 | 0 | Hydrophobic |
| C18 | CB | LYS- 123 | 3.86 | 0 | Hydrophobic |
| N2 | O | LYS- 123 | 3.04 | 134.13 | H-Bond (Ligand Donor) |
| C11 | CD2 | LEU- 124 | 4.4 | 0 | Hydrophobic |
| C22 | CD1 | PHE- 126 | 3.33 | 0 | Hydrophobic |
| C17 | CB | PHE- 126 | 4.49 | 0 | Hydrophobic |
| C13 | CE2 | PHE- 127 | 3.43 | 0 | Hydrophobic |
| O16 | N | SER- 209 | 2.99 | 147.15 | H-Bond (Protein Donor) |
