1.350 Å
X-ray
2001-05-22
Name: | Flavodoxin |
---|---|
ID: | FLAV_DESVH |
AC: | P00323 |
Organism: | Desulfovibrio vulgaris |
Reign: | Bacteria |
TaxID: | 882 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 18.492 |
---|---|
Number of residues: | 37 |
Including | |
Standard Amino Acids: | 34 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.379 | 266.625 |
% Hydrophobic | % Polar |
---|---|
45.57 | 54.43 |
According to VolSite |
HET Code: | FMN |
---|---|
Formula: | C17H19N4O9P |
Molecular weight: | 454.328 g/mol |
DrugBank ID: | DB03247 |
Buried Surface Area: | 67.93 % |
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 |
---|---|---|
26.3592 | 10.4731 | 81.8615 |
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 |
O1P | OG | SER- 10 | 2.71 | 170.32 | H-Bond (Protein Donor) |
O3P | N | THR- 11 | 2.83 | 160.34 | H-Bond (Protein Donor) |
O2P | N | THR- 12 | 2.85 | 137.08 | H-Bond (Protein Donor) |
O2P | OG1 | THR- 12 | 2.55 | 166.19 | H-Bond (Protein Donor) |
O4' | ND2 | ASN- 14 | 2.77 | 165.75 | H-Bond (Protein Donor) |
O2P | N | ASN- 14 | 2.96 | 158.52 | H-Bond (Protein Donor) |
O1P | OG1 | THR- 15 | 2.79 | 144.22 | H-Bond (Protein Donor) |
O1P | N | THR- 15 | 2.71 | 160.92 | H-Bond (Protein Donor) |
O1P | OG | SER- 58 | 3.48 | 134.57 | H-Bond (Protein Donor) |
O3P | OG | SER- 58 | 2.59 | 152.66 | H-Bond (Protein Donor) |
C5' | CB | SER- 58 | 3.84 | 0 | Hydrophobic |
O2' | O | THR- 59 | 2.72 | 160.23 | H-Bond (Ligand Donor) |
C7M | CZ3 | TRP- 60 | 4.49 | 0 | Hydrophobic |
C2' | CZ2 | TRP- 60 | 4.46 | 0 | Hydrophobic |
C5' | CZ2 | TRP- 60 | 3.81 | 0 | Hydrophobic |
C8 | CZ3 | TRP- 60 | 3.49 | 0 | Hydrophobic |
O4 | N | ASP- 62 | 3.18 | 137.13 | H-Bond (Protein Donor) |
N5 | N | ASP- 62 | 3.4 | 137.56 | H-Bond (Protein Donor) |
C6 | CB | ASP- 62 | 4.42 | 0 | Hydrophobic |
C4' | CB | CYS- 93 | 3.83 | 0 | Hydrophobic |
N1 | N | ASP- 95 | 3.22 | 122.32 | H-Bond (Protein Donor) |
O2 | N | ASP- 95 | 3.1 | 162.78 | H-Bond (Protein Donor) |
C1' | CB | ASP- 95 | 4.18 | 0 | Hydrophobic |
C1' | CE2 | TYR- 98 | 4.04 | 0 | Hydrophobic |
N3 | O | TYR- 100 | 3.09 | 168.92 | H-Bond (Ligand Donor) |
O2 | N | CYS- 102 | 2.84 | 168.83 | H-Bond (Protein Donor) |
O4' | O | HOH- 155 | 2.6 | 165.6 | H-Bond (Ligand Donor) |
O4 | O | HOH- 164 | 2.71 | 179.97 | H-Bond (Protein Donor) |