1.900 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: | 18.138 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 28 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MN MN |
Ligandability | Volume (Å3) |
---|---|
0.609 | 479.250 |
% Hydrophobic | % Polar |
---|---|
40.14 | 59.86 |
According to VolSite |
HET Code: | B23 |
---|---|
Formula: | C11H6NO5 |
Molecular weight: | 232.169 g/mol |
DrugBank ID: | DB07408 |
Buried Surface Area: | 71.94 % |
Polar Surface area: | 99.09 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 0 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 2 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 3 |
X | Y | Z |
---|---|---|
-3.15806 | -0.0728235 | 9.08253 |
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 |
CAK | CB | TYR- 62 | 4.45 | 0 | Hydrophobic |
CAI | CD2 | TYR- 62 | 3.48 | 0 | Hydrophobic |
CAI | CB | HIS- 63 | 3.81 | 0 | Hydrophobic |
CAK | CB | TYR- 65 | 4.34 | 0 | Hydrophobic |
OAO | NE2 | HIS- 178 | 2.8 | 141.22 | H-Bond (Protein Donor) |
OAM | NE2 | HIS- 178 | 3.23 | 125.92 | H-Bond (Protein Donor) |
CAK | CZ3 | TRP- 221 | 3.39 | 0 | Hydrophobic |
OAN | MN | MN- 300 | 2.33 | 0 | Metal Acceptor |
OAO | MN | MN- 300 | 2.23 | 0 | Metal Acceptor |
OAN | MN | MN- 301 | 2.15 | 0 | Metal Acceptor |