1.670 Å
X-ray
2012-08-09
Name: | Anthranilate phosphoribosyltransferase |
---|---|
ID: | TRPD_MYCTU |
AC: | P9WFX5 |
Organism: | Mycobacterium tuberculosis |
Reign: | Bacteria |
TaxID: | 83332 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 16.455 |
---|---|
Number of residues: | 32 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.753 | 914.625 |
% Hydrophobic | % Polar |
---|---|
40.59 | 59.41 |
According to VolSite |
HET Code: | 636 |
---|---|
Formula: | C16H13NO4 |
Molecular weight: | 283.279 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 62.18 % |
Polar Surface area: | 92.29 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 1 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 4 |
X | Y | Z |
---|---|---|
2.32748 | -28.3009 | 33.6517 |
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 |
CX4 | CE | MET- 86 | 4.45 | 0 | Hydrophobic |
C3 | CE | MET- 86 | 4.08 | 0 | Hydrophobic |
C5 | CG2 | VAL- 106 | 4.28 | 0 | Hydrophobic |
OX1 | ND2 | ASN- 138 | 2.82 | 154.78 | H-Bond (Protein Donor) |
CY5 | CB | ASN- 138 | 3.9 | 0 | Hydrophobic |
CX3 | CB | ALA- 179 | 3.63 | 0 | Hydrophobic |
CY6 | CB | ALA- 179 | 3.82 | 0 | Hydrophobic |
CX4 | CB | ALA- 179 | 3.41 | 0 | Hydrophobic |
CX6 | CG | PRO- 180 | 4.17 | 0 | Hydrophobic |
CX4 | CB | HIS- 183 | 3.65 | 0 | Hydrophobic |
C3 | CE2 | TYR- 186 | 4.16 | 0 | Hydrophobic |
CX4 | CD2 | TYR- 186 | 3.5 | 0 | Hydrophobic |
CX5 | CB | TYR- 186 | 4.28 | 0 | Hydrophobic |
OX2 | NH1 | ARG- 193 | 3.28 | 135.24 | H-Bond (Protein Donor) |
OY1 | NH1 | ARG- 193 | 3.07 | 140.92 | H-Bond (Protein Donor) |
OY1 | NH2 | ARG- 193 | 2.88 | 152.27 | H-Bond (Protein Donor) |
OY2 | NH2 | ARG- 193 | 3.38 | 143.49 | H-Bond (Protein Donor) |
OY1 | CZ | ARG- 193 | 3.4 | 0 | Ionic (Protein Cationic) |
OY2 | O | HOH- 520 | 2.8 | 179.97 | H-Bond (Protein Donor) |