1.760 Å
X-ray
2000-05-11
Name: | Glycogen phosphorylase, muscle form |
---|---|
ID: | PYGM_RABIT |
AC: | P00489 |
Organism: | Oryctolagus cuniculus |
Reign: | Eukaryota |
TaxID: | 9986 |
EC Number: | 2.4.1.1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 24.040 |
---|---|
Number of residues: | 27 |
Including | |
Standard Amino Acids: | 24 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.645 | 651.375 |
% Hydrophobic | % Polar |
---|---|
51.30 | 48.70 |
According to VolSite |
HET Code: | CPB |
---|---|
Formula: | C21H20ClNO5 |
Molecular weight: | 401.840 g/mol |
DrugBank ID: | DB03496 |
Buried Surface Area: | 45.69 % |
Polar Surface area: | 94.26 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 3 |
Rings: | 4 |
Aromatic rings: | 2 |
Anionic atoms: | 1 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
39.372 | 36.4362 | 29.7552 |
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 |
C14 | CE1 | PHE- 285 | 4.02 | 0 | Hydrophobic |
C13 | CZ | PHE- 285 | 3.9 | 0 | Hydrophobic |
C10 | CB | PHE- 285 | 4.31 | 0 | Hydrophobic |
DuAr | DuAr | PHE- 285 | 3.67 | 0 | Aromatic Face/Face |
C25 | CD1 | ILE- 380 | 3.59 | 0 | Hydrophobic |
C25 | CG | GLU- 382 | 3.35 | 0 | Hydrophobic |
CL1 | CZ | TYR- 613 | 3.68 | 0 | Hydrophobic |
C5 | CB | TYR- 613 | 3.65 | 0 | Hydrophobic |
O4 | O | HOH- 1035 | 2.62 | 179.97 | H-Bond (Protein Donor) |
O5 | O | HOH- 1209 | 3.16 | 179.98 | H-Bond (Protein Donor) |