1.300 Å
X-ray
2012-12-28
Name: | Methionine aminopeptidase 1 |
---|---|
ID: | MAP11_HUMAN |
AC: | P53582 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 14.053 |
---|---|
Number of residues: | 24 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.216 | 327.375 |
% Hydrophobic | % Polar |
---|---|
49.48 | 50.52 |
According to VolSite |
HET Code: | SHX |
---|---|
Formula: | C19H18ClN5O |
Molecular weight: | 367.832 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 49.08 % |
Polar Surface area: | 93.79 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 2 |
Rings: | 3 |
Aromatic rings: | 3 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 6 |
X | Y | Z |
---|---|---|
20.7607 | -6.56885 | 15.2348 |
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 |
C2 | CB | PRO- 192 | 4.22 | 0 | Hydrophobic |
C10 | CE2 | TYR- 195 | 4.19 | 0 | Hydrophobic |
C3 | CB | PHE- 198 | 4.02 | 0 | Hydrophobic |
C2 | SG | CYS- 203 | 4.02 | 0 | Hydrophobic |
C17 | CE1 | TYR- 300 | 3.49 | 0 | Hydrophobic |
DuAr | DuAr | HIS- 310 | 3.38 | 0 | Aromatic Face/Face |
DuAr | DuAr | HIS- 310 | 3.38 | 0 | Aromatic Face/Face |
CL | CB | HIS- 310 | 4.14 | 0 | Hydrophobic |
C3 | CZ3 | TRP- 353 | 3.36 | 0 | Hydrophobic |
C15 | CZ3 | TRP- 353 | 3.41 | 0 | Hydrophobic |