1.750 Å
X-ray
2015-05-01
Name: | Putative b-glycan phosphorylase |
---|---|
ID: | Q21MB1_SACD2 |
AC: | Q21MB1 |
Organism: | Saccharophagus degradans |
Reign: | Bacteria |
TaxID: | 203122 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 22.086 |
---|---|
Number of residues: | 20 |
Including | |
Standard Amino Acids: | 19 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.972 | 1603.125 |
% Hydrophobic | % Polar |
---|---|
40.63 | 59.37 |
According to VolSite |
HET Code: | LGC |
---|---|
Formula: | C6H10O6 |
Molecular weight: | 178.140 g/mol |
DrugBank ID: | DB04564 |
Buried Surface Area: | 63.04 % |
Polar Surface area: | 107.22 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 4 |
Rings: | 1 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 1 |
X | Y | Z |
---|---|---|
-66.7313 | 27.1627 | 3.56542 |
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 |
O3 | NH2 | ARG- 349 | 2.97 | 159.84 | H-Bond (Protein Donor) |
O2 | ND2 | ASN- 350 | 3 | 156.3 | H-Bond (Protein Donor) |
O3 | OD1 | ASN- 350 | 2.69 | 137.31 | H-Bond (Ligand Donor) |
O4 | O | TRP- 470 | 2.66 | 168.2 | H-Bond (Ligand Donor) |
C5 | CZ2 | TRP- 470 | 4.23 | 0 | Hydrophobic |
C6 | CH2 | TRP- 470 | 3.75 | 0 | Hydrophobic |
O6 | N | ASP- 472 | 2.86 | 164.97 | H-Bond (Protein Donor) |
C6 | CG | GLU- 619 | 3.86 | 0 | Hydrophobic |
O6 | OE2 | GLU- 619 | 2.73 | 148.42 | H-Bond (Ligand Donor) |
C6 | CE2 | TYR- 624 | 4.11 | 0 | Hydrophobic |