1.600 Å
X-ray
2007-06-12
| Name: | Methionine aminopeptidase |
|---|---|
| ID: | MAP1_ECOLI |
| AC: | P0AE18 |
| Organism: | Escherichia coli |
| Reign: | Bacteria |
| TaxID: | 83333 |
| EC Number: | / |
| Chain Name: | Percentage of Residues within binding site |
|---|---|
| A | 100 % |
| B-Factor: | 9.279 |
|---|---|
| Number of residues: | 26 |
| Including | |
| Standard Amino Acids: | 24 |
| Non Standard Amino Acids: | 2 |
| Water Molecules: | 0 |
| Cofactors: | |
| Metals: | MN MN |
| Ligandability | Volume (Å3) |
|---|---|
| 0.385 | 357.750 |
| % Hydrophobic | % Polar |
|---|---|
| 44.34 | 55.66 |
| According to VolSite | |

| HET Code: | B21 |
|---|---|
| Formula: | C12H9O4 |
| Molecular weight: | 217.197 g/mol |
| DrugBank ID: | DB07407 |
| Buried Surface Area: | 62.49 % |
| Polar Surface area: | 62.5 Å2 |
| Number of | |
|---|---|
| H-Bond Acceptors: | 3 |
| H-Bond Donors: | 0 |
| Rings: | 2 |
| Aromatic rings: | 2 |
| Anionic atoms: | 1 |
| Cationic atoms: | 0 |
| Rule of Five Violation: | 0 |
| Rotatable Bonds: | 3 |
| X | Y | Z |
|---|---|---|
| -3.33819 | -0.761375 | 8.81081 |
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 |
| CAL | CD2 | TYR- 62 | 3.62 | 0 | Hydrophobic |
| CAL | CG | TYR- 65 | 3.61 | 0 | Hydrophobic |
| OAM | NE2 | HIS- 178 | 3.18 | 135.08 | H-Bond (Protein Donor) |
| OAO | NE2 | HIS- 178 | 2.88 | 143.08 | H-Bond (Protein Donor) |
| CAL | CZ3 | TRP- 221 | 4.41 | 0 | Hydrophobic |
| OAO | MN | MN- 301 | 2.26 | 0 | Metal Acceptor |
| OAN | MN | MN- 301 | 2.37 | 0 | Metal Acceptor |
| OAN | MN | MN- 302 | 2.07 | 0 | Metal Acceptor |