1.820 Å
X-ray
2008-04-18
Name: | N-acetyllactosaminide alpha-1,3-galactosyltransferase |
---|---|
ID: | GGTA1_BOVIN |
AC: | P14769 |
Organism: | Bos taurus |
Reign: | Eukaryota |
TaxID: | 9913 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 19.761 |
---|---|
Number of residues: | 39 |
Including | |
Standard Amino Acids: | 36 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 2 |
Cofactors: | |
Metals: | MN |
Ligandability | Volume (Å3) |
---|---|
0.676 | 1029.375 |
% Hydrophobic | % Polar |
---|---|
43.28 | 56.72 |
According to VolSite |
HET Code: | GDU |
---|---|
Formula: | C15H22N2O17P2 |
Molecular weight: | 564.286 g/mol |
DrugBank ID: | DB03501 |
Buried Surface Area: | 71.81 % |
Polar Surface area: | 316.82 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 7 |
Rings: | 3 |
Aromatic rings: | 0 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 9 |
X | Y | Z |
---|---|---|
5.17542 | 23.4667 | 23.1517 |
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 |
O2D | O | PHE- 134 | 2.56 | 156.87 | H-Bond (Ligand Donor) |
N3 | O | VAL- 136 | 2.94 | 171.48 | H-Bond (Ligand Donor) |
O2 | N | VAL- 136 | 2.83 | 156.4 | H-Bond (Protein Donor) |
C3D | CE1 | TYR- 139 | 3.73 | 0 | Hydrophobic |
C2D | CD1 | TYR- 139 | 3.66 | 0 | Hydrophobic |
O2A | OH | TYR- 139 | 2.73 | 146.83 | H-Bond (Protein Donor) |
C6' | CZ3 | TRP- 195 | 4.34 | 0 | Hydrophobic |
C1D | CG2 | ILE- 198 | 3.97 | 0 | Hydrophobic |
C5D | CB | SER- 199 | 4.15 | 0 | Hydrophobic |
C6' | CB | SER- 199 | 4.45 | 0 | Hydrophobic |
O3' | NH2 | ARG- 202 | 2.87 | 144.8 | H-Bond (Protein Donor) |
C3D | CB | ASP- 225 | 4.48 | 0 | Hydrophobic |
O2' | OD2 | ASP- 225 | 2.82 | 176.83 | H-Bond (Ligand Donor) |
O3' | OD1 | ASP- 225 | 3.02 | 161.22 | H-Bond (Ligand Donor) |
O3D | N | VAL- 226 | 3 | 142.72 | H-Bond (Protein Donor) |
C2D | CG1 | VAL- 226 | 3.65 | 0 | Hydrophobic |
O3D | OD1 | ASP- 227 | 2.9 | 143.63 | H-Bond (Ligand Donor) |
C3' | CB | ALA- 281 | 3.97 | 0 | Hydrophobic |
C6' | CB | HIS- 315 | 3.85 | 0 | Hydrophobic |
O6' | ND1 | HIS- 315 | 2.83 | 141.72 | H-Bond (Protein Donor) |
O4' | OD2 | ASP- 316 | 2.79 | 135.27 | H-Bond (Ligand Donor) |
O2A | NH2 | ARG- 365 | 3.03 | 154.79 | H-Bond (Protein Donor) |
O2A | CZ | ARG- 365 | 3.92 | 0 | Ionic (Protein Cationic) |
O1A | MN | MN- 1366 | 2.38 | 0 | Metal Acceptor |
O2B | MN | MN- 1366 | 2.61 | 0 | Metal Acceptor |
O2D | O | HOH- 2205 | 2.85 | 179.97 | H-Bond (Protein Donor) |
O3' | O | HOH- 2302 | 3.27 | 129.89 | H-Bond (Protein Donor) |