2.900 Å
X-ray
2013-01-24
| Name: | Ribosomal protein S6--L-glutamate ligase |
|---|---|
| ID: | RIMK_ECOLI |
| AC: | P0C0U4 |
| Organism: | Escherichia coli |
| Reign: | Bacteria |
| TaxID: | 83333 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 85.878 |
|---|---|
| Number of residues: | 27 |
| Including | |
| Standard Amino Acids: | 27 |
| Non Standard Amino Acids: | 0 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | |
| Ligandability | Volume (Å3) |
|---|---|
| 1.205 | 911.250 |
| % Hydrophobic | % Polar |
|---|---|
| 54.07 | 45.93 |
| According to VolSite | |

| HET Code: | ADP |
|---|---|
| Formula: | C10H12N5O10P2 |
| Molecular weight: | 424.177 g/mol |
| DrugBank ID: | - |
| Buried Surface Area: | 68.38 % |
| Polar Surface area: | 260.7 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 14 |
| H-Bond Donors: | 3 |
| Rings: | 3 |
| Aromatic rings: | 2 |
| Anionic atoms: | 3 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 1 |
| Rotatable Bonds: | 6 |
| X | Y | Z |
|---|---|---|
| -11.6919 | 45.3094 | 68.4382 |
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 |
| O2A | NZ | LYS- 141 | 3.08 | 141.95 | H-Bond (Protein Donor) |
| N7 | NZ | LYS- 141 | 3.38 | 134.55 | H-Bond (Protein Donor) |
| O2A | NZ | LYS- 141 | 3.08 | 0 | Ionic (Protein Cationic) |
| C5' | CG2 | VAL- 151 | 4.21 | 0 | Hydrophobic |
| N6 | OE1 | GLU- 178 | 2.99 | 173.61 | H-Bond (Ligand Donor) |
| N6 | O | TYR- 179 | 2.95 | 145.07 | H-Bond (Ligand Donor) |
| O1B | CZ | ARG- 203 | 3.91 | 0 | Ionic (Protein Cationic) |
| O1B | NH2 | ARG- 203 | 3.39 | 146.68 | H-Bond (Protein Donor) |
| C1' | CE2 | PHE- 210 | 3.6 | 0 | Hydrophobic |
| C2' | CB | SER- 212 | 4.13 | 0 | Hydrophobic |
| O2B | ND2 | ASN- 213 | 2.77 | 138.39 | H-Bond (Protein Donor) |
| C2' | SD | MET- 259 | 3.92 | 0 | Hydrophobic |