2.100 Å
X-ray
2006-10-05
Name: | Lactate oxidase |
---|---|
ID: | Q44467_9LACT |
AC: | Q44467 |
Organism: | Aerococcus viridans |
Reign: | Bacteria |
TaxID: | 1377 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
H | 100 % |
B-Factor: | 9.400 |
---|---|
Number of residues: | 44 |
Including | |
Standard Amino Acids: | 42 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.024 | 604.125 |
% Hydrophobic | % Polar |
---|---|
41.90 | 58.10 |
According to VolSite |
HET Code: | FMN |
---|---|
Formula: | C17H19N4O9P |
Molecular weight: | 454.328 g/mol |
DrugBank ID: | DB03247 |
Buried Surface Area: | 83.11 % |
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 |
---|---|---|
45.833 | 117.571 | 70.294 |
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 |
C7M | CE2 | TYR- 40 | 3.83 | 0 | Hydrophobic |
C7M | CG1 | ILE- 41 | 4.11 | 0 | Hydrophobic |
C3' | CB | ALA- 92 | 3.93 | 0 | Hydrophobic |
O2' | O | PRO- 93 | 2.82 | 173.57 | H-Bond (Ligand Donor) |
C2' | CG1 | ILE- 94 | 3.87 | 0 | Hydrophobic |
C6 | CG2 | ILE- 94 | 3.51 | 0 | Hydrophobic |
C9 | CG1 | ILE- 94 | 3.68 | 0 | Hydrophobic |
N5 | N | ALA- 95 | 3.31 | 157.67 | H-Bond (Protein Donor) |
O4 | OG | SER- 122 | 2.88 | 140.68 | H-Bond (Protein Donor) |
N3 | OE1 | GLN- 144 | 2.95 | 162.04 | H-Bond (Ligand Donor) |
O2 | OG1 | THR- 172 | 2.68 | 158.55 | H-Bond (Protein Donor) |
O2 | NZ | LYS- 241 | 2.81 | 139.14 | H-Bond (Protein Donor) |
O2' | NZ | LYS- 241 | 2.88 | 155.98 | H-Bond (Protein Donor) |
O3' | OG | SER- 263 | 3.43 | 131.81 | H-Bond (Protein Donor) |
C9 | CD | ARG- 268 | 3.58 | 0 | Hydrophobic |
O3' | OD1 | ASP- 296 | 3.23 | 130.9 | H-Bond (Ligand Donor) |
O3' | OD2 | ASP- 296 | 2.67 | 163.6 | H-Bond (Ligand Donor) |
C5' | CB | ASP- 296 | 4.31 | 0 | Hydrophobic |
C5' | CB | SER- 297 | 4.33 | 0 | Hydrophobic |
O3P | N | GLY- 298 | 3.09 | 157.68 | H-Bond (Protein Donor) |
O2P | CZ | ARG- 300 | 3.62 | 0 | Ionic (Protein Cationic) |
O3P | CZ | ARG- 300 | 3.91 | 0 | Ionic (Protein Cationic) |
O2P | NH2 | ARG- 300 | 2.8 | 173.5 | H-Bond (Protein Donor) |
O3P | NH1 | ARG- 300 | 3 | 171.29 | H-Bond (Protein Donor) |
C8M | CG | ARG- 320 | 3.51 | 0 | Hydrophobic |
O1P | N | ARG- 320 | 2.77 | 167.03 | H-Bond (Protein Donor) |
O2P | NH1 | ARG- 320 | 2.69 | 132.2 | H-Bond (Protein Donor) |
O2P | CZ | ARG- 320 | 3.87 | 0 | Ionic (Protein Cationic) |
C7M | CD2 | LEU- 323 | 4.36 | 0 | Hydrophobic |
O3P | O | HOH- 2136 | 2.83 | 158.63 | H-Bond (Protein Donor) |
O3P | O | HOH- 2159 | 2.66 | 132.44 | H-Bond (Protein Donor) |