1.750 Å
X-ray
2009-11-07
Name: | Uncharacterized protein |
---|---|
ID: | Q5L808_BACFN |
AC: | Q5L808 |
Organism: | Bacteroides fragilis |
Reign: | Bacteria |
TaxID: | 272559 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 24.710 |
---|---|
Number of residues: | 32 |
Including | |
Standard Amino Acids: | 31 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.634 | 428.625 |
% Hydrophobic | % Polar |
---|---|
42.52 | 57.48 |
According to VolSite |
HET Code: | FMN |
---|---|
Formula: | C17H19N4O9P |
Molecular weight: | 454.328 g/mol |
DrugBank ID: | DB03247 |
Buried Surface Area: | 70.28 % |
Polar Surface area: | 217.05 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 12 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
27.7505 | -2.03155 | 30.0669 |
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 |
O3P | OG | SER- 12 | 2.57 | 175.01 | H-Bond (Protein Donor) |
O2P | N | CYS- 13 | 2.79 | 149.66 | H-Bond (Protein Donor) |
O1P | N | SER- 14 | 3.07 | 121.12 | H-Bond (Protein Donor) |
O2P | N | SER- 14 | 2.87 | 169.81 | H-Bond (Protein Donor) |
C5' | CB | VAL- 16 | 4.46 | 0 | Hydrophobic |
O1P | N | VAL- 16 | 2.89 | 161.62 | H-Bond (Protein Donor) |
O5' | OG1 | THR- 17 | 3.46 | 137 | H-Bond (Protein Donor) |
O3P | N | THR- 17 | 2.77 | 160.85 | H-Bond (Protein Donor) |
O3P | OG1 | THR- 17 | 2.8 | 147.21 | H-Bond (Protein Donor) |
C8M | CB | LEU- 46 | 4.02 | 0 | Hydrophobic |
C8M | CE3 | TRP- 48 | 3.86 | 0 | Hydrophobic |
C7 | CB | TRP- 48 | 4.48 | 0 | Hydrophobic |
C7M | CB | SER- 55 | 3.62 | 0 | Hydrophobic |
C2' | CB | PRO- 86 | 4.16 | 0 | Hydrophobic |
C5' | CB | PRO- 86 | 3.68 | 0 | Hydrophobic |
O2' | O | VAL- 87 | 2.74 | 160.47 | H-Bond (Ligand Donor) |
C7M | CD2 | TRP- 88 | 3.97 | 0 | Hydrophobic |
C8M | CE2 | TRP- 88 | 4.17 | 0 | Hydrophobic |
C6 | CB | TRP- 88 | 3.93 | 0 | Hydrophobic |
N5 | N | TRP- 89 | 2.95 | 158.11 | H-Bond (Protein Donor) |
O4 | N | TYR- 90 | 2.9 | 135.24 | H-Bond (Protein Donor) |
C4' | CB | THR- 115 | 4.43 | 0 | Hydrophobic |
O4' | OG1 | THR- 115 | 2.76 | 159.42 | H-Bond (Ligand Donor) |
N1 | N | GLY- 117 | 3.06 | 158.61 | H-Bond (Protein Donor) |
O2 | N | SER- 119 | 2.76 | 174.33 | H-Bond (Protein Donor) |
N3 | OG | SER- 119 | 2.9 | 157.41 | H-Bond (Ligand Donor) |