2.500 Å
X-ray
2004-02-10
Name: | WbpP |
---|---|
ID: | Q8KN66_PSEAI |
AC: | Q8KN66 |
Organism: | Pseudomonas aeruginosa |
Reign: | Bacteria |
TaxID: | 287 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 32.957 |
---|---|
Number of residues: | 47 |
Including | |
Standard Amino Acids: | 41 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 5 |
Cofactors: | NAD |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.004 | 1269.000 |
% Hydrophobic | % Polar |
---|---|
39.10 | 60.90 |
According to VolSite |
HET Code: | UPG |
---|---|
Formula: | C15H22N2O17P2 |
Molecular weight: | 564.286 g/mol |
DrugBank ID: | DB01861 |
Buried Surface Area: | 63.66 % |
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 |
---|---|---|
40.423 | 7.49764 | 91.4081 |
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 |
O4' | N | SER- 103 | 3.42 | 160.63 | H-Bond (Protein Donor) |
C6' | CB | SER- 142 | 4.23 | 0 | Hydrophobic |
O6' | OG | SER- 142 | 2.64 | 140.21 | H-Bond (Protein Donor) |
C6' | CB | SER- 144 | 4.03 | 0 | Hydrophobic |
C6' | CE2 | TYR- 166 | 3.46 | 0 | Hydrophobic |
O2B | ND2 | ASN- 195 | 3.18 | 138.87 | H-Bond (Protein Donor) |
C1C | CG2 | VAL- 210 | 4.36 | 0 | Hydrophobic |
C4C | CB | VAL- 210 | 4.42 | 0 | Hydrophobic |
C5C | CG1 | VAL- 210 | 3.88 | 0 | Hydrophobic |
O2A | N | VAL- 210 | 3 | 171.25 | H-Bond (Protein Donor) |
O4 | NE1 | TRP- 214 | 3.43 | 132.25 | H-Bond (Protein Donor) |
N3 | O | TYR- 225 | 2.64 | 162.72 | H-Bond (Ligand Donor) |
O2 | N | ASN- 227 | 2.77 | 171.66 | H-Bond (Protein Donor) |
O2C | ND2 | ASN- 227 | 3.07 | 162.35 | H-Bond (Protein Donor) |
O2B | NE | ARG- 234 | 3.27 | 152.56 | H-Bond (Protein Donor) |
C1C | CD1 | LEU- 271 | 3.87 | 0 | Hydrophobic |
C4C | CD2 | LEU- 271 | 3.98 | 0 | Hydrophobic |
O1A | NH2 | ARG- 299 | 2.83 | 156.48 | H-Bond (Protein Donor) |
O1B | NH2 | ARG- 299 | 3.34 | 124.93 | H-Bond (Protein Donor) |
O1A | CZ | ARG- 299 | 3.84 | 0 | Ionic (Protein Cationic) |
O3C | OD1 | ASP- 302 | 2.97 | 142.89 | H-Bond (Ligand Donor) |
O3C | OD2 | ASP- 302 | 2.79 | 148.51 | H-Bond (Ligand Donor) |
C2' | C4N | NAD- 342 | 4.38 | 0 | Hydrophobic |
C3' | C3N | NAD- 342 | 4.35 | 0 | Hydrophobic |
C6' | C5N | NAD- 342 | 4.06 | 0 | Hydrophobic |
C4' | C4N | NAD- 342 | 3.69 | 0 | Hydrophobic |
O1A | O | HOH- 374 | 2.63 | 159.05 | H-Bond (Protein Donor) |
O2C | O | HOH- 385 | 2.87 | 164.74 | H-Bond (Protein Donor) |