2.400 Å
X-ray
2001-03-08
Name: | S-adenosylmethionine decarboxylase proenzyme |
---|---|
ID: | DCAM_HUMAN |
AC: | P17707 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 4.1.1.50 |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 29 % |
A | 71 % |
B-Factor: | 23.196 |
---|---|
Number of residues: | 23 |
Including | |
Standard Amino Acids: | 23 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.315 | 425.250 |
% Hydrophobic | % Polar |
---|---|
39.68 | 60.32 |
According to VolSite |
HET Code: | MGB |
---|---|
Formula: | C5H14N8 |
Molecular weight: | 186.218 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 63.6 % |
Polar Surface area: | 152 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 6 |
Rings: | 0 |
Aromatic rings: | 0 |
Anionic atoms: | 0 |
Cationic atoms: | 2 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 5 |
X | Y | Z |
---|---|---|
-17.0312 | -6.00215 | 7.03015 |
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 | CE2 | PHE- 7 | 4.26 | 0 | Hydrophobic |
N12 | O | LEU- 65 | 2.73 | 140.08 | H-Bond (Ligand Donor) |
C6 | CD1 | PHE- 223 | 3.89 | 0 | Hydrophobic |
N12 | OG | SER- 229 | 2.58 | 138.58 | H-Bond (Ligand Donor) |
N1 | OE2 | GLU- 247 | 3.35 | 124.03 | H-Bond (Ligand Donor) |
N1 | OE1 | GLU- 247 | 2.81 | 136.2 | H-Bond (Ligand Donor) |