2.500 Å
X-ray
1996-03-12
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 |
---|---|
B | 100 % |
B-Factor: | 22.650 |
---|---|
Number of residues: | 27 |
Including | |
Standard Amino Acids: | 23 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.975 | 1542.375 |
% Hydrophobic | % Polar |
---|---|
43.76 | 56.24 |
According to VolSite |
HET Code: | NTZ |
---|---|
Formula: | C6H10N4O4 |
Molecular weight: | 202.168 g/mol |
DrugBank ID: | DB02471 |
Buried Surface Area: | 70.43 % |
Polar Surface area: | 124.52 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 4 |
Rings: | 2 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 1 |
X | Y | Z |
---|---|---|
83.8464 | 5.83571 | 74.7879 |
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 |
C6 | CD2 | LEU- 139 | 3.91 | 0 | Hydrophobic |
O6 | ND1 | HIS- 377 | 2.9 | 159.2 | H-Bond (Ligand Donor) |
O2 | OG1 | THR- 378 | 3.24 | 141.12 | H-Bond (Protein Donor) |
O4 | ND2 | ASN- 484 | 3.28 | 122.93 | H-Bond (Protein Donor) |
O6 | ND2 | ASN- 484 | 2.72 | 145 | H-Bond (Protein Donor) |
O3 | OE1 | GLU- 672 | 2.71 | 147.96 | H-Bond (Ligand Donor) |
C2 | CB | ALA- 673 | 4.25 | 0 | Hydrophobic |
C4 | CB | SER- 674 | 4.35 | 0 | Hydrophobic |
O3 | N | SER- 674 | 3.27 | 169.85 | H-Bond (Protein Donor) |
O3 | N | GLY- 675 | 3.24 | 129.91 | H-Bond (Protein Donor) |
O4 | N | GLY- 675 | 2.92 | 145.56 | H-Bond (Protein Donor) |