1.780 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: | 18.984 |
---|---|
Number of residues: | 23 |
Including | |
Standard Amino Acids: | 23 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.488 | 344.250 |
% Hydrophobic | % Polar |
---|---|
51.96 | 48.04 |
According to VolSite |
HET Code: | PVP |
---|---|
Formula: | C16H21ClN5O |
Molecular weight: | 334.824 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 44.07 % |
Polar Surface area: | 66.58 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 2 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 0 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 4 |
X | Y | Z |
---|---|---|
-2.29361 | -6.82461 | 15.792 |
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 | 4.05 | 0 | Hydrophobic |
C13 | CE2 | TYR- 195 | 3.84 | 0 | Hydrophobic |
C10 | CZ | TYR- 195 | 4.44 | 0 | Hydrophobic |
C13 | CD1 | TYR- 196 | 4.18 | 0 | Hydrophobic |
C3 | CB | PHE- 198 | 3.85 | 0 | Hydrophobic |
C2 | SG | CYS- 203 | 3.8 | 0 | Hydrophobic |
C10 | CB | HIS- 310 | 3.88 | 0 | Hydrophobic |
CL | CB | HIS- 310 | 4.26 | 0 | Hydrophobic |
DuAr | DuAr | HIS- 310 | 3.44 | 0 | Aromatic Face/Face |
DuAr | DuAr | HIS- 310 | 3.44 | 0 | Aromatic Face/Face |
C4 | CZ3 | TRP- 353 | 3.32 | 0 | Hydrophobic |