1.950 Å
X-ray
2006-03-07
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: | 18.904 |
---|---|
Number of residues: | 32 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MN MN |
Ligandability | Volume (Å3) |
---|---|
0.951 | 421.875 |
% Hydrophobic | % Polar |
---|---|
57.60 | 42.40 |
According to VolSite |
HET Code: | A19 |
---|---|
Formula: | C13H8BrClNO4S |
Molecular weight: | 389.629 g/mol |
DrugBank ID: | DB07309 |
Buried Surface Area: | 65.49 % |
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 |
---|---|---|
16.8998 | 29.6492 | 18.2254 |
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 |
CL1 | CB | ALA- 230 | 3.44 | 0 | Hydrophobic |
O20 | NE2 | HIS- 231 | 2.99 | 167.48 | H-Bond (Protein Donor) |
CL1 | CD1 | LEU- 328 | 3.7 | 0 | Hydrophobic |
C2 | CD2 | LEU- 328 | 3.68 | 0 | Hydrophobic |
C13 | CG2 | ILE- 338 | 3.74 | 0 | Hydrophobic |
C17 | CG1 | ILE- 338 | 3.9 | 0 | Hydrophobic |
C13 | CB | HIS- 339 | 4.22 | 0 | Hydrophobic |
CL1 | CZ | PHE- 366 | 3.53 | 0 | Hydrophobic |
C14 | CE | MET- 384 | 3.91 | 0 | Hydrophobic |
BR18 | CB | ALA- 414 | 3.8 | 0 | Hydrophobic |
BR18 | CG | TYR- 444 | 3.89 | 0 | Hydrophobic |
C3 | CD1 | LEU- 447 | 3.85 | 0 | Hydrophobic |
O21 | MN | MN- 481 | 2.45 | 0 | Metal Acceptor |