1.300 Å
X-ray
2006-04-21
Name: | UDP-N-acetylenolpyruvoylglucosamine reductase |
---|---|
ID: | MURB_THET8 |
AC: | Q5SJC8 |
Organism: | Thermus thermophilus |
Reign: | Bacteria |
TaxID: | 300852 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 13.341 |
---|---|
Number of residues: | 55 |
Including | |
Standard Amino Acids: | 53 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.000 | 1272.375 |
% Hydrophobic | % Polar |
---|---|
29.97 | 70.03 |
According to VolSite |
HET Code: | FAD |
---|---|
Formula: | C27H31N9O15P2 |
Molecular weight: | 783.534 g/mol |
DrugBank ID: | DB03147 |
Buried Surface Area: | 72.19 % |
Polar Surface area: | 381.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 22 |
H-Bond Donors: | 7 |
Rings: | 6 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
-0.256868 | -1.13396 | -0.336981 |
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 |
C8M | CB | THR- 15 | 4.18 | 0 | Hydrophobic |
O2B | O | VAL- 43 | 2.65 | 151.53 | H-Bond (Ligand Donor) |
O2A | N | GLY- 45 | 2.79 | 132.1 | H-Bond (Protein Donor) |
O1P | N | ASN- 46 | 2.94 | 168.11 | H-Bond (Protein Donor) |
O2A | N | GLY- 47 | 2.84 | 145 | H-Bond (Protein Donor) |
C2' | CB | SER- 48 | 4.14 | 0 | Hydrophobic |
C8M | CB | SER- 48 | 3.9 | 0 | Hydrophobic |
O2' | OG | SER- 48 | 2.69 | 158 | H-Bond (Ligand Donor) |
O2P | N | SER- 48 | 2.87 | 159.5 | H-Bond (Protein Donor) |
O2P | OG | SER- 48 | 2.6 | 176.64 | H-Bond (Protein Donor) |
O1A | N | ASN- 49 | 2.83 | 163.91 | H-Bond (Protein Donor) |
C5B | CB | ASN- 49 | 4.35 | 0 | Hydrophobic |
C5' | CB | ASN- 49 | 4.12 | 0 | Hydrophobic |
C2' | CB | ASN- 49 | 4.02 | 0 | Hydrophobic |
C5B | CD2 | LEU- 50 | 4.21 | 0 | Hydrophobic |
C3B | CD2 | LEU- 50 | 4.13 | 0 | Hydrophobic |
C3' | CG2 | ILE- 104 | 4.3 | 0 | Hydrophobic |
C8 | CG | PRO- 105 | 3.51 | 0 | Hydrophobic |
C4' | CB | ALA- 106 | 3.59 | 0 | Hydrophobic |
O1P | N | GLN- 107 | 2.91 | 148.07 | H-Bond (Protein Donor) |
C4B | CG | LYS- 113 | 4.17 | 0 | Hydrophobic |
C1B | CG | LYS- 113 | 3.71 | 0 | Hydrophobic |
C4B | CG | MET- 114 | 4.06 | 0 | Hydrophobic |
C3' | CB | ALA- 116 | 4.33 | 0 | Hydrophobic |
O2 | N | GLY- 117 | 3 | 158.06 | H-Bond (Protein Donor) |
N3 | O | GLY- 117 | 2.72 | 177.83 | H-Bond (Ligand Donor) |
N6A | O | VAL- 161 | 2.93 | 165.97 | H-Bond (Ligand Donor) |
N1A | N | VAL- 161 | 2.9 | 145.98 | H-Bond (Protein Donor) |
O4 | NH2 | ARG- 187 | 3.16 | 130.8 | H-Bond (Protein Donor) |
O4 | NH1 | ARG- 187 | 2.88 | 140.54 | H-Bond (Protein Donor) |
N5 | NH2 | ARG- 187 | 2.92 | 152.51 | H-Bond (Protein Donor) |
O3B | OE2 | GLU- 264 | 3.41 | 132.05 | H-Bond (Ligand Donor) |
O3B | OE1 | GLU- 264 | 2.53 | 170.25 | H-Bond (Ligand Donor) |
C2B | CZ2 | TRP- 266 | 4.33 | 0 | Hydrophobic |