1.250 Å
X-ray
2010-11-11
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: | 10.177 |
---|---|
Number of residues: | 31 |
Including | |
Standard Amino Acids: | 28 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | MN MN |
Ligandability | Volume (Å3) |
---|---|
0.657 | 442.125 |
% Hydrophobic | % Polar |
---|---|
45.80 | 54.20 |
According to VolSite |
HET Code: | Y16 |
---|---|
Formula: | C14H26N2O6 |
Molecular weight: | 318.366 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 70.5 % |
Polar Surface area: | 142.1 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 5 |
Rings: | 0 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 9 |
X | Y | Z |
---|---|---|
-6.64918 | -43.8585 | 4.16791 |
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 |
C10 | CG2 | THR- 94 | 3.93 | 0 | Hydrophobic |
C08 | CE2 | TYR- 97 | 3.63 | 0 | Hydrophobic |
C10 | CD2 | TYR- 97 | 3.45 | 0 | Hydrophobic |
C09 | CD1 | PHE- 100 | 4.3 | 0 | Hydrophobic |
C09 | SG | CYS- 105 | 3.66 | 0 | Hydrophobic |
C14 | SG | CYS- 113 | 4.09 | 0 | Hydrophobic |
O4 | NE2 | HIS- 114 | 3.38 | 121.6 | H-Bond (Protein Donor) |
O6 | NE2 | HIS- 114 | 2.73 | 156.7 | H-Bond (Protein Donor) |
C09 | CB | HIS- 114 | 4.48 | 0 | Hydrophobic |
C14 | CB | PHE- 202 | 4.01 | 0 | Hydrophobic |
N1 | O | THR- 203 | 2.83 | 143.24 | H-Bond (Ligand Donor) |
O5 | N | THR- 203 | 2.89 | 150.32 | H-Bond (Protein Donor) |
C04 | CZ | PHE- 211 | 3.96 | 0 | Hydrophobic |
C10 | CE2 | PHE- 211 | 4.12 | 0 | Hydrophobic |
O2 | NE2 | HIS- 212 | 2.67 | 164.69 | H-Bond (Ligand Donor) |
O3 | OE1 | GLU- 238 | 2.54 | 145.8 | H-Bond (Ligand Donor) |
C14 | SD | MET- 240 | 3.96 | 0 | Hydrophobic |
C08 | CZ3 | TRP- 255 | 3.8 | 0 | Hydrophobic |
O2 | MN | MN- 287 | 2.3 | 0 | Metal Acceptor |
O3 | MN | MN- 287 | 2.21 | 0 | Metal Acceptor |
O1 | MN | MN- 288 | 2.15 | 0 | Metal Acceptor |
O3 | MN | MN- 288 | 2.21 | 0 | Metal Acceptor |