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 |
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 |