2.000 Å
X-ray
2007-07-30
Name: | Urocanate hydratase |
---|---|
ID: | HUTU_PSEPU |
AC: | P25080 |
Organism: | Pseudomonas putida |
Reign: | Bacteria |
TaxID: | 303 |
EC Number: | 4.2.1.49 |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 24.204 |
---|---|
Number of residues: | 67 |
Including | |
Standard Amino Acids: | 65 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.709 | 742.500 |
% Hydrophobic | % Polar |
---|---|
42.27 | 57.73 |
According to VolSite |
HET Code: | NAD |
---|---|
Formula: | C21H26N7O14P2 |
Molecular weight: | 662.417 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 85.39 % |
Polar Surface area: | 343.54 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 18 |
H-Bond Donors: | 6 |
Rings: | 5 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 1 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 11 |
X | Y | Z |
---|---|---|
-0.527864 | 19.8707 | 4.05184 |
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 |
O3 | N | GLY- 53 | 3.31 | 124.38 | H-Bond (Protein Donor) |
O2N | N | GLY- 53 | 2.95 | 131.95 | H-Bond (Protein Donor) |
O2A | N | GLY- 54 | 2.86 | 150.91 | H-Bond (Protein Donor) |
O2D | NE2 | GLN- 131 | 3.12 | 153.33 | H-Bond (Protein Donor) |
C4N | CD1 | ILE- 145 | 3.26 | 0 | Hydrophobic |
O1A | N | GLY- 177 | 3.33 | 162.56 | H-Bond (Protein Donor) |
O1N | N | MET- 178 | 3.11 | 137.58 | H-Bond (Protein Donor) |
O2N | N | MET- 178 | 3.16 | 148.1 | H-Bond (Protein Donor) |
C5N | CG | MET- 178 | 3.76 | 0 | Hydrophobic |
O1N | N | GLY- 179 | 2.9 | 173.14 | H-Bond (Protein Donor) |
O3B | OE1 | GLU- 197 | 2.69 | 170.22 | H-Bond (Ligand Donor) |
O2B | OE2 | GLU- 197 | 2.53 | 155.96 | H-Bond (Ligand Donor) |
O2B | OG | SER- 198 | 3.1 | 140.11 | H-Bond (Protein Donor) |
N3A | N | SER- 198 | 3.38 | 133.52 | H-Bond (Protein Donor) |
O2B | NE2 | GLN- 199 | 2.77 | 162.76 | H-Bond (Protein Donor) |
N6A | OD1 | ASN- 243 | 2.98 | 155.57 | H-Bond (Ligand Donor) |
N1A | N | ALA- 244 | 2.92 | 173.35 | H-Bond (Protein Donor) |
O4D | NE2 | GLN- 264 | 3.01 | 159.18 | H-Bond (Protein Donor) |
C4D | CG | GLN- 264 | 3.78 | 0 | Hydrophobic |
O2A | OG | SER- 266 | 2.84 | 171.48 | H-Bond (Protein Donor) |
C5B | CB | SER- 266 | 3.89 | 0 | Hydrophobic |
C3D | CB | SER- 266 | 4.31 | 0 | Hydrophobic |
O3D | ND1 | HIS- 268 | 2.77 | 171.78 | H-Bond (Ligand Donor) |
N7A | N | LEU- 275 | 2.99 | 172.82 | H-Bond (Protein Donor) |
C2B | CZ3 | TRP- 281 | 3.86 | 0 | Hydrophobic |
N7N | O | TYR- 323 | 2.96 | 139.97 | H-Bond (Ligand Donor) |
C4D | CB | ASN- 325 | 4.14 | 0 | Hydrophobic |
O2D | O | GLY- 493 | 2.69 | 140.34 | H-Bond (Ligand Donor) |
O1N | O | HOH- 2192 | 2.73 | 179.99 | H-Bond (Protein Donor) |