2.560 Å
X-ray
2012-09-19
Name: | Chromate reductase |
---|---|
ID: | D5QFC5_KOMHA |
AC: | D5QFC5 |
Organism: | Komagataeibacter hansenii ATCC 23769 |
Reign: | Bacteria |
TaxID: | 714995 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
H | 19 % |
I | 81 % |
B-Factor: | 89.522 |
---|---|
Number of residues: | 41 |
Including | |
Standard Amino Acids: | 39 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.772 | 867.375 |
% Hydrophobic | % Polar |
---|---|
38.91 | 61.09 |
According to VolSite |
HET Code: | FMN |
---|---|
Formula: | C17H19N4O9P |
Molecular weight: | 454.328 g/mol |
DrugBank ID: | DB03247 |
Buried Surface Area: | 60.54 % |
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 |
---|---|---|
-62.492 | 38.8458 | 23.5141 |
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 |
O2P | OG | SER- 15 | 2.73 | 168.76 | H-Bond (Protein Donor) |
O4' | NH2 | ARG- 17 | 3.38 | 135.68 | H-Bond (Protein Donor) |
O1P | NH2 | ARG- 17 | 2.63 | 140.83 | H-Bond (Protein Donor) |
O2P | NE | ARG- 17 | 3.15 | 153.39 | H-Bond (Protein Donor) |
O1P | CZ | ARG- 17 | 3.49 | 0 | Ionic (Protein Cationic) |
O2P | CZ | ARG- 17 | 3.95 | 0 | Ionic (Protein Cationic) |
O3P | OG | SER- 20 | 2.7 | 174.92 | H-Bond (Protein Donor) |
O1P | N | PHE- 21 | 3.09 | 158.73 | H-Bond (Protein Donor) |
O3P | N | ASN- 22 | 3 | 163.94 | H-Bond (Protein Donor) |
O3P | ND2 | ASN- 22 | 2.77 | 171.15 | H-Bond (Protein Donor) |
C8M | CE2 | TYR- 51 | 3.57 | 0 | Hydrophobic |
C5' | CB | PRO- 82 | 3.92 | 0 | Hydrophobic |
N3 | OE2 | GLU- 83 | 2.81 | 129.54 | H-Bond (Ligand Donor) |
C7M | CG | TYR- 84 | 4.32 | 0 | Hydrophobic |
C8M | CE1 | TYR- 84 | 4.42 | 0 | Hydrophobic |
C5' | CE1 | TYR- 84 | 4.47 | 0 | Hydrophobic |
C6 | CB | TYR- 84 | 3.78 | 0 | Hydrophobic |
N5 | N | ASN- 85 | 2.76 | 159.51 | H-Bond (Protein Donor) |
O4 | N | TYR- 86 | 2.69 | 161.43 | H-Bond (Protein Donor) |
C7M | CB | ASP- 97 | 4.46 | 0 | Hydrophobic |
O2 | OG | SER- 118 | 3.1 | 153.88 | H-Bond (Protein Donor) |
C3' | CG | PRO- 119 | 3.98 | 0 | Hydrophobic |
C1' | CG1 | VAL- 167 | 3.79 | 0 | Hydrophobic |
C3' | CG1 | VAL- 167 | 4.46 | 0 | Hydrophobic |
O2 | O | HOH- 308 | 2.84 | 179.96 | H-Bond (Protein Donor) |