2.090 Å
X-ray
2012-11-12
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: | 40.586 |
---|---|
Number of residues: | 32 |
Including | |
Standard Amino Acids: | 32 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.539 | 297.000 |
% Hydrophobic | % Polar |
---|---|
55.68 | 44.32 |
According to VolSite |
HET Code: | 1AY |
---|---|
Formula: | C28H30Cl2N5 |
Molecular weight: | 507.477 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 42.4 % |
Polar Surface area: | 67.31 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 2 |
Rings: | 4 |
Aromatic rings: | 4 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 11 |
X | Y | Z |
---|---|---|
20.8104 | 19.3374 | 18.5115 |
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 |
C17 | CB | GLU- 128 | 3.8 | 0 | Hydrophobic |
C32 | CG | GLN- 129 | 3.74 | 0 | Hydrophobic |
C33 | CD | LYS- 132 | 3.74 | 0 | Hydrophobic |
C32 | CB | LYS- 132 | 3.31 | 0 | Hydrophobic |
CL8 | CB | PRO- 192 | 4 | 0 | Hydrophobic |
C6 | CD2 | TYR- 195 | 3.03 | 0 | Hydrophobic |
CL8 | CD1 | PHE- 198 | 3.38 | 0 | Hydrophobic |
CL8 | SG | CYS- 203 | 3.94 | 0 | Hydrophobic |
C12 | CB | HIS- 310 | 4.49 | 0 | Hydrophobic |
DuAr | DuAr | HIS- 310 | 3.4 | 0 | Aromatic Face/Face |
DuAr | DuAr | HIS- 310 | 3.4 | 0 | Aromatic Face/Face |
CL8 | CZ3 | TRP- 353 | 4.41 | 0 | Hydrophobic |