2.200 Å
X-ray
2004-05-28
Name: | Phenylalanine-4-hydroxylase |
---|---|
ID: | PH4H_HUMAN |
AC: | P00439 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 1.14.16.1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 33.236 |
---|---|
Number of residues: | 28 |
Including | |
Standard Amino Acids: | 26 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | FE |
Ligandability | Volume (Å3) |
---|---|
0.810 | 364.500 |
% Hydrophobic | % Polar |
---|---|
60.19 | 39.81 |
According to VolSite |
HET Code: | H2B |
---|---|
Formula: | C9H15N5O3 |
Molecular weight: | 241.247 g/mol |
DrugBank ID: | DB02562 |
Buried Surface Area: | 60.87 % |
Polar Surface area: | 135.88 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 4 |
H-Bond Donors: | 6 |
Rings: | 2 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 2 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
-6.65206 | 24.9956 | 6.877 |
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 |
N2 | O | GLY- 247 | 2.83 | 123.19 | H-Bond (Ligand Donor) |
N1 | N | LEU- 249 | 3.09 | 160.07 | H-Bond (Protein Donor) |
N8 | O | LEU- 249 | 2.81 | 162.64 | H-Bond (Ligand Donor) |
O10 | OG | SER- 251 | 2.62 | 149.43 | H-Bond (Protein Donor) |
C11 | CD2 | PHE- 254 | 3.41 | 0 | Hydrophobic |
C11 | CD2 | LEU- 255 | 3.63 | 0 | Hydrophobic |
C10 | CB | ALA- 322 | 4.08 | 0 | Hydrophobic |
C11 | CD1 | TYR- 325 | 3.55 | 0 | Hydrophobic |
N2 | O | HOH- 429 | 3.23 | 122.75 | H-Bond (Ligand Donor) |