1.400 Å
X-ray
2009-08-30
Name: | Methionine aminopeptidase 2 |
---|---|
ID: | MAP12_MYCTU |
AC: | P9WK19 |
Organism: | Mycobacterium tuberculosis |
Reign: | Bacteria |
TaxID: | 83332 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 7.862 |
---|---|
Number of residues: | 23 |
Including | |
Standard Amino Acids: | 21 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MN MN |
Ligandability | Volume (Å3) |
---|---|
0.675 | 519.750 |
% Hydrophobic | % Polar |
---|---|
49.35 | 50.65 |
According to VolSite |
HET Code: | FCD |
---|---|
Formula: | C11H6ClO3 |
Molecular weight: | 221.617 g/mol |
DrugBank ID: | DB02909 |
Buried Surface Area: | 64.46 % |
Polar Surface area: | 53.27 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 2 |
H-Bond Donors: | 0 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
-35.2806 | -29.7845 | -5.5202 |
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 |
CL2 | CG2 | THR- 94 | 3.99 | 0 | Hydrophobic |
CL2 | CD2 | TYR- 97 | 4.07 | 0 | Hydrophobic |
C5 | CD2 | TYR- 97 | 3.47 | 0 | Hydrophobic |
C4 | CD | LYS- 98 | 4.15 | 0 | Hydrophobic |
CL2 | CG | PHE- 100 | 3.83 | 0 | Hydrophobic |
CL2 | SG | CYS- 105 | 4.19 | 0 | Hydrophobic |
OA | NE2 | HIS- 212 | 3.34 | 121.46 | H-Bond (Protein Donor) |
OB | NE2 | HIS- 212 | 2.69 | 165.88 | H-Bond (Protein Donor) |
C5 | CZ3 | TRP- 255 | 3.45 | 0 | Hydrophobic |
OXT | MN | MN- 286 | 2.14 | 0 | Metal Acceptor |
OB | MN | MN- 287 | 2.41 | 0 | Metal Acceptor |
OXT | MN | MN- 287 | 2.22 | 0 | Metal Acceptor |