1.550 Å
X-ray
2015-06-13
Name: | Histo-blood group ABO system transferase |
---|---|
ID: | BGAT_HUMAN |
AC: | P16442 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 22.363 |
---|---|
Number of residues: | 31 |
Including | |
Standard Amino Acids: | 28 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | MN |
Ligandability | Volume (Å3) |
---|---|
0.063 | 546.750 |
% Hydrophobic | % Polar |
---|---|
42.59 | 57.41 |
According to VolSite |
HET Code: | GDU |
---|---|
Formula: | C15H22N2O17P2 |
Molecular weight: | 564.286 g/mol |
DrugBank ID: | DB03501 |
Buried Surface Area: | 57.87 % |
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 |
---|---|---|
13.0981 | -20.1627 | -6.96611 |
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 |
C1D | CB | PHE- 121 | 4.33 | 0 | Hydrophobic |
O2D | O | PHE- 121 | 2.57 | 171.09 | H-Bond (Ligand Donor) |
N3 | O | ILE- 123 | 2.82 | 167.7 | H-Bond (Ligand Donor) |
O2 | N | ILE- 123 | 2.85 | 162.06 | H-Bond (Protein Donor) |
C3D | CE1 | TYR- 126 | 3.81 | 0 | Hydrophobic |
C2D | CD1 | TYR- 126 | 3.66 | 0 | Hydrophobic |
C3D | CB | ASP- 211 | 4.43 | 0 | Hydrophobic |
O2D | N | VAL- 212 | 3.5 | 149.41 | H-Bond (Protein Donor) |
O3D | N | VAL- 212 | 3.12 | 143.63 | H-Bond (Protein Donor) |
C2D | CG1 | VAL- 212 | 3.73 | 0 | Hydrophobic |
O3D | OD1 | ASP- 213 | 2.78 | 133.2 | H-Bond (Ligand Donor) |
C6' | CE3 | TRP- 300 | 4.2 | 0 | Hydrophobic |
C4' | CB | HIS- 301 | 3.92 | 0 | Hydrophobic |
O3' | OD2 | ASP- 302 | 2.64 | 155.16 | H-Bond (Ligand Donor) |
O3' | N | GLU- 303 | 2.89 | 145.98 | H-Bond (Protein Donor) |
C2' | CB | GLU- 303 | 3.65 | 0 | Hydrophobic |
O1A | NZ | LYS- 346 | 2.77 | 0 | Ionic (Protein Cationic) |
O2A | NZ | LYS- 346 | 3.06 | 0 | Ionic (Protein Cationic) |
O2A | MN | MN- 401 | 2.1 | 0 | Metal Acceptor |
O2B | MN | MN- 401 | 2.69 | 0 | Metal Acceptor |
O2D | O | HOH- 525 | 2.71 | 179.96 | H-Bond (Protein Donor) |