2.080 Å
X-ray
2012-03-27
Name: | UDP-glucose 6-dehydrogenase |
---|---|
ID: | UGDH_HUMAN |
AC: | O60701 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 1.1.1.22 |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 95 % |
C | 5 % |
B-Factor: | 31.111 |
---|---|
Number of residues: | 43 |
Including | |
Standard Amino Acids: | 41 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.579 | 965.250 |
% Hydrophobic | % Polar |
---|---|
41.96 | 58.04 |
According to VolSite |
HET Code: | UPG |
---|---|
Formula: | C15H22N2O17P2 |
Molecular weight: | 564.286 g/mol |
DrugBank ID: | DB01861 |
Buried Surface Area: | 75.08 % |
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 |
---|---|---|
55.2167 | 16.6911 | 49.0331 |
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 |
C6' | CG | GLU- 161 | 4.29 | 0 | Hydrophobic |
O4' | O | PHE- 162 | 3.41 | 163.09 | H-Bond (Ligand Donor) |
C3' | CB | ALA- 164 | 4.31 | 0 | Hydrophobic |
O2B | N | GLU- 165 | 2.98 | 172.14 | H-Bond (Protein Donor) |
O4' | NZ | LYS- 220 | 3.1 | 147.8 | H-Bond (Protein Donor) |
O6' | NZ | LYS- 220 | 3.42 | 120.24 | H-Bond (Protein Donor) |
O6' | ND2 | ASN- 224 | 3.12 | 156.29 | H-Bond (Protein Donor) |
C2' | CD1 | LEU- 227 | 4.14 | 0 | Hydrophobic |
C1C | CD1 | ILE- 231 | 3.93 | 0 | Hydrophobic |
O2' | NH2 | ARG- 260 | 3.28 | 123.38 | H-Bond (Protein Donor) |
O2' | NH1 | ARG- 260 | 2.67 | 143.13 | H-Bond (Protein Donor) |
O3' | NH2 | ARG- 260 | 2.71 | 157.97 | H-Bond (Protein Donor) |
N3 | O | LYS- 267 | 3 | 176.5 | H-Bond (Ligand Donor) |
O4 | N | LYS- 267 | 3.19 | 153.67 | H-Bond (Protein Donor) |
O2 | OG | SER- 269 | 2.8 | 162.01 | H-Bond (Protein Donor) |
C1C | CB | PHE- 272 | 3.86 | 0 | Hydrophobic |
C4C | CB | PHE- 272 | 3.76 | 0 | Hydrophobic |
O3C | N | GLY- 273 | 3.05 | 158.75 | H-Bond (Protein Donor) |
C5' | CB | CYS- 276 | 4.45 | 0 | Hydrophobic |
C6' | SG | CYS- 276 | 3.41 | 0 | Hydrophobic |
C4C | CD2 | PHE- 277 | 4.3 | 0 | Hydrophobic |
C5C | CE2 | PHE- 277 | 3.67 | 0 | Hydrophobic |
C1' | CE1 | PHE- 277 | 3.71 | 0 | Hydrophobic |
O3C | O | PHE- 338 | 2.57 | 164.76 | H-Bond (Ligand Donor) |
C5C | CE2 | PHE- 338 | 4.01 | 0 | Hydrophobic |
C3C | CD2 | PHE- 338 | 3.65 | 0 | Hydrophobic |
O1A | NZ | LYS- 339 | 2.69 | 168.15 | H-Bond (Protein Donor) |
O1A | NZ | LYS- 339 | 2.69 | 0 | Ionic (Protein Cationic) |
C3C | CB | LYS- 339 | 4 | 0 | Hydrophobic |
O2C | NH1 | ARG- 442 | 2.65 | 143.13 | H-Bond (Protein Donor) |
O2C | NH2 | ARG- 442 | 2.97 | 130.01 | H-Bond (Protein Donor) |
O1B | O | HOH- 601 | 2.58 | 145.6 | H-Bond (Protein Donor) |