2.450 Å
X-ray
2014-08-28
Name: | UDP-N-acetylglucosamine 1-carboxyvinyltransferase |
---|---|
ID: | MURA_VIBCH |
AC: | Q9KP62 |
Organism: | Vibrio cholerae serotype O1 |
Reign: | Bacteria |
TaxID: | 243277 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 25.116 |
---|---|
Number of residues: | 41 |
Including | |
Standard Amino Acids: | 40 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.721 | 1272.375 |
% Hydrophobic | % Polar |
---|---|
36.07 | 63.93 |
According to VolSite |
HET Code: | UD1 |
---|---|
Formula: | C17H25N3O17P2 |
Molecular weight: | 605.338 g/mol |
DrugBank ID: | DB03397 |
Buried Surface Area: | 59.29 % |
Polar Surface area: | 325.69 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: | 10 |
X | Y | Z |
---|---|---|
-38.5095 | -15.2944 | -19.1434 |
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 |
C8' | CB | ASN- 24 | 3.45 | 0 | Hydrophobic |
O3' | ND2 | ASN- 24 | 3.38 | 127.79 | H-Bond (Protein Donor) |
C8' | CH2 | TRP- 96 | 3.38 | 0 | Hydrophobic |
O2B | CZ | ARG- 121 | 3.73 | 0 | Ionic (Protein Cationic) |
O2B | NH2 | ARG- 121 | 2.84 | 162.95 | H-Bond (Protein Donor) |
N3 | OD1 | ASP- 124 | 2.74 | 151.14 | H-Bond (Ligand Donor) |
O4 | N | LEU- 125 | 2.88 | 151.91 | H-Bond (Protein Donor) |
O2 | NZ | LYS- 161 | 3.18 | 145.21 | H-Bond (Protein Donor) |
O1A | OG | SER- 163 | 2.82 | 159.9 | H-Bond (Protein Donor) |
C1' | CB | VAL- 164 | 4.23 | 0 | Hydrophobic |
C8' | CG1 | VAL- 164 | 4.47 | 0 | Hydrophobic |
C6' | CG2 | VAL- 164 | 3.94 | 0 | Hydrophobic |
O2A | N | VAL- 164 | 2.79 | 148.1 | H-Bond (Protein Donor) |
O1A | N | GLY- 165 | 3.41 | 149.61 | H-Bond (Protein Donor) |
O1B | N | GLY- 165 | 2.86 | 125.97 | H-Bond (Protein Donor) |
C6' | CG2 | THR- 305 | 4.29 | 0 | Hydrophobic |
O3' | OD2 | ASP- 306 | 2.88 | 162.41 | H-Bond (Ligand Donor) |
O4' | OD2 | ASP- 306 | 3.25 | 145.4 | H-Bond (Ligand Donor) |
O4' | OD1 | ASP- 306 | 2.65 | 144.64 | H-Bond (Ligand Donor) |
O3B | O | ILE- 328 | 2.94 | 174.83 | H-Bond (Ligand Donor) |
C5B | CG2 | ILE- 328 | 3.71 | 0 | Hydrophobic |
C5' | CZ | PHE- 329 | 4.24 | 0 | Hydrophobic |
C5B | CZ | PHE- 329 | 4.41 | 0 | Hydrophobic |
C3B | CE1 | PHE- 329 | 3.71 | 0 | Hydrophobic |
O2' | O | HOH- 621 | 3.22 | 148.22 | H-Bond (Protein Donor) |