1.980 Å
X-ray
2012-09-13
Name: | 2-methyl-3-hydroxypyridine-5-carboxylic acid oxygenase |
---|---|
ID: | Q988D3_RHILO |
AC: | Q988D3 |
Organism: | Rhizobium loti |
Reign: | Bacteria |
TaxID: | 266835 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
C | 100 % |
B-Factor: | 21.605 |
---|---|
Number of residues: | 68 |
Including | |
Standard Amino Acids: | 61 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 7 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.741 | 1674.000 |
% Hydrophobic | % Polar |
---|---|
42.54 | 57.46 |
According to VolSite |
HET Code: | FAD |
---|---|
Formula: | C27H31N9O15P2 |
Molecular weight: | 783.534 g/mol |
DrugBank ID: | DB03147 |
Buried Surface Area: | 63.12 % |
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 |
---|---|---|
-57.3282 | -13.4895 | -19.8279 |
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 |
C4' | CD2 | PHE- 21 | 4.3 | 0 | Hydrophobic |
O1P | N | ALA- 22 | 2.83 | 159.32 | H-Bond (Protein Donor) |
O2B | OE1 | GLU- 41 | 2.94 | 166.12 | H-Bond (Ligand Donor) |
N3A | N | LYS- 42 | 3.19 | 142.25 | H-Bond (Protein Donor) |
N3 | O | TYR- 54 | 2.78 | 158.81 | H-Bond (Ligand Donor) |
O4 | N | TYR- 54 | 2.91 | 168.35 | H-Bond (Protein Donor) |
O2' | NH1 | ARG- 106 | 2.97 | 143.98 | H-Bond (Protein Donor) |
O2' | NH2 | ARG- 106 | 2.96 | 145.24 | H-Bond (Protein Donor) |
N6A | O | ALA- 130 | 3.08 | 168.8 | H-Bond (Ligand Donor) |
N1A | N | ALA- 130 | 3.05 | 148.27 | H-Bond (Protein Donor) |
C7M | CD2 | LEU- 179 | 3.64 | 0 | Hydrophobic |
C7M | CD | ARG- 181 | 3.72 | 0 | Hydrophobic |
C7M | CE2 | TYR- 270 | 4.16 | 0 | Hydrophobic |
O3' | OD1 | ASP- 288 | 2.76 | 173.32 | H-Bond (Ligand Donor) |
C5' | CB | ASP- 288 | 4.13 | 0 | Hydrophobic |
O2P | N | ASP- 288 | 2.89 | 162.43 | H-Bond (Protein Donor) |
C7M | CG | PRO- 295 | 4.17 | 0 | Hydrophobic |
C6 | CB | PRO- 295 | 3.66 | 0 | Hydrophobic |
N1 | N | ALA- 301 | 3.01 | 169.4 | H-Bond (Protein Donor) |
O2 | N | ALA- 301 | 2.92 | 124.36 | H-Bond (Protein Donor) |
C4' | CB | ALA- 301 | 4.04 | 0 | Hydrophobic |
C2' | CB | ALA- 301 | 4.14 | 0 | Hydrophobic |
O2 | N | GLY- 302 | 3.05 | 144.48 | H-Bond (Protein Donor) |
O1P | O | HOH- 502 | 2.61 | 170.54 | H-Bond (Protein Donor) |
O2P | O | HOH- 503 | 2.7 | 179.99 | H-Bond (Protein Donor) |
O2A | O | HOH- 506 | 2.65 | 179.98 | H-Bond (Protein Donor) |