2.200 Å
X-ray
2005-09-12
Name: | Phospholipase A2, major isoenzyme |
---|---|
ID: | PA21B_PIG |
AC: | P00592 |
Organism: | Sus scrofa |
Reign: | Eukaryota |
TaxID: | 9823 |
EC Number: | 3.1.1.4 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 44.738 |
---|---|
Number of residues: | 28 |
Including | |
Standard Amino Acids: | 26 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | CL CA |
Ligandability | Volume (Å3) |
---|---|
1.272 | 820.125 |
% Hydrophobic | % Polar |
---|---|
57.61 | 42.39 |
According to VolSite |
HET Code: | TUD |
---|---|
Formula: | C26H44NO6S |
Molecular weight: | 498.696 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 56.61 % |
Polar Surface area: | 135.14 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 3 |
Rings: | 4 |
Aromatic rings: | 0 |
Anionic atoms: | 1 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
41.035 | 21.1939 | 15.7077 |
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 |
C2 | CD1 | LEU- 2 | 4.07 | 0 | Hydrophobic |
C1 | CD2 | PHE- 5 | 3.81 | 0 | Hydrophobic |
C19 | CE2 | PHE- 5 | 4.13 | 0 | Hydrophobic |
C2 | CG | ARG- 6 | 3.6 | 0 | Hydrophobic |
C3 | CD | ARG- 6 | 4.28 | 0 | Hydrophobic |
O3 | NH2 | ARG- 6 | 3.22 | 167.1 | H-Bond (Protein Donor) |
C21 | CG2 | ILE- 9 | 3.98 | 0 | Hydrophobic |
C11 | CD1 | ILE- 9 | 3.51 | 0 | Hydrophobic |
C21 | CD1 | ILE- 13 | 4.04 | 0 | Hydrophobic |
C26 | CE | MET- 20 | 3.96 | 0 | Hydrophobic |
C2 | CD2 | PHE- 22 | 4.09 | 0 | Hydrophobic |
C4 | CB | PHE- 22 | 4.15 | 0 | Hydrophobic |
C9 | CB | PHE- 22 | 4.08 | 0 | Hydrophobic |
C12 | CG | PHE- 22 | 4 | 0 | Hydrophobic |
C14 | CB | PHE- 22 | 3.96 | 0 | Hydrophobic |
C23 | CE1 | PHE- 22 | 4.44 | 0 | Hydrophobic |
C7 | CB | PHE- 22 | 4.14 | 0 | Hydrophobic |
C17 | CD1 | PHE- 22 | 4.23 | 0 | Hydrophobic |
O7 | O | ASN- 23 | 2.7 | 139.71 | H-Bond (Ligand Donor) |
C15 | CB | TYR- 25 | 3.55 | 0 | Hydrophobic |
C15 | CB | CYS- 29 | 3.98 | 0 | Hydrophobic |
C18 | SG | CYS- 29 | 4.08 | 0 | Hydrophobic |
C8 | CB | CYS- 29 | 4.16 | 0 | Hydrophobic |
C16 | CD2 | LEU- 41 | 3.99 | 0 | Hydrophobic |
C18 | CD1 | LEU- 41 | 4.32 | 0 | Hydrophobic |
C20 | CD2 | LEU- 41 | 4.28 | 0 | Hydrophobic |
C18 | SG | CYS- 45 | 3.75 | 0 | Hydrophobic |
C18 | CZ | PHE- 106 | 3.56 | 0 | Hydrophobic |
C21 | CB | PHE- 106 | 3.99 | 0 | Hydrophobic |
C11 | CE2 | PHE- 106 | 3.86 | 0 | Hydrophobic |
C16 | CE2 | TYR- 111 | 4.26 | 0 | Hydrophobic |
C26 | CZ | TYR- 111 | 3.55 | 0 | Hydrophobic |
C22 | CD2 | TYR- 111 | 3.92 | 0 | Hydrophobic |
O28 | NZ | LYS- 116 | 2.84 | 138.72 | H-Bond (Protein Donor) |
O28 | NZ | LYS- 116 | 2.84 | 0 | Ionic (Protein Cationic) |