2.200 Å
X-ray
2008-05-07
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: | 18.055 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 28 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MN MN |
Ligandability | Volume (Å3) |
---|---|
0.687 | 330.750 |
% Hydrophobic | % Polar |
---|---|
52.04 | 47.96 |
According to VolSite |
HET Code: | W29 |
---|---|
Formula: | C12H12O2S |
Molecular weight: | 220.287 g/mol |
DrugBank ID: | DB08718 |
Buried Surface Area: | 69.04 % |
Polar Surface area: | 68.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 2 |
H-Bond Donors: | 2 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
-2.94347 | 13.7465 | 8.91013 |
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 |
O2 | MN | MN- 1 | 2.36 | 0 | Metal Acceptor |
O1 | MN | MN- 1 | 2.42 | 0 | Metal Acceptor |
O2 | MN | MN- 2 | 2.01 | 0 | Metal Acceptor |
C11 | CB | CYS- 59 | 4.47 | 0 | Hydrophobic |
C11 | CD2 | TYR- 62 | 3.68 | 0 | Hydrophobic |
C11 | CB | TYR- 65 | 4.23 | 0 | Hydrophobic |
C12 | CG | TYR- 65 | 3.55 | 0 | Hydrophobic |
C04 | SG | CYS- 70 | 4.32 | 0 | Hydrophobic |
C12 | SG | CYS- 70 | 3.41 | 0 | Hydrophobic |
O1 | NE2 | HIS- 178 | 2.52 | 135.44 | H-Bond (Ligand Donor) |