1.850 Å
X-ray
2005-02-17
Name: | Methionine aminopeptidase 2 |
---|---|
ID: | MAP2_HUMAN |
AC: | P50579 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 19.517 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 27 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | MN MN |
Ligandability | Volume (Å3) |
---|---|
1.005 | 438.750 |
% Hydrophobic | % Polar |
---|---|
59.23 | 40.77 |
According to VolSite |
HET Code: | A41 |
---|---|
Formula: | C14H12NO4S |
Molecular weight: | 290.314 g/mol |
DrugBank ID: | DB07313 |
Buried Surface Area: | 64.42 % |
Polar Surface area: | 94.68 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 1 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 4 |
X | Y | Z |
---|---|---|
16.9036 | 29.6255 | 18.206 |
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 |
C1 | CB | ALA- 230 | 4.01 | 0 | Hydrophobic |
O18 | NE2 | HIS- 231 | 2.9 | 162.82 | H-Bond (Protein Donor) |
C1 | CD2 | LEU- 328 | 3.61 | 0 | Hydrophobic |
C13 | CG2 | ILE- 338 | 3.77 | 0 | Hydrophobic |
C16 | CG1 | ILE- 338 | 4.02 | 0 | Hydrophobic |
C12 | CB | HIS- 339 | 4.04 | 0 | Hydrophobic |
C13 | CE | MET- 384 | 3.79 | 0 | Hydrophobic |
C20 | CB | ALA- 414 | 3.89 | 0 | Hydrophobic |
C20 | CG | TYR- 444 | 3.85 | 0 | Hydrophobic |
C2 | CD1 | LEU- 447 | 3.7 | 0 | Hydrophobic |
O19 | MN | MN- 481 | 2.35 | 0 | Metal Acceptor |