1.950 Å
X-ray
2005-09-21
Name: | Diamine acetyltransferase 1 |
---|---|
ID: | SAT1_HUMAN |
AC: | P21673 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 21.206 |
---|---|
Number of residues: | 39 |
Including | |
Standard Amino Acids: | 37 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.292 | 624.375 |
% Hydrophobic | % Polar |
---|---|
34.59 | 65.41 |
According to VolSite |
HET Code: | ACO |
---|---|
Formula: | C23H34N7O17P3S |
Molecular weight: | 805.539 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 55.74 % |
Polar Surface area: | 429.68 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 22 |
H-Bond Donors: | 5 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 20 |
X | Y | Z |
---|---|---|
22.8959 | 57.5709 | 47.9934 |
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 |
C6P | CD1 | LEU- 24 | 4.35 | 0 | Hydrophobic |
C6P | CE1 | TYR- 27 | 3.8 | 0 | Hydrophobic |
CH3 | CG | LEU- 91 | 3.93 | 0 | Hydrophobic |
CEP | CE1 | PHE- 94 | 3.73 | 0 | Hydrophobic |
N4P | O | PHE- 94 | 2.9 | 148.84 | H-Bond (Ligand Donor) |
C6P | CD1 | PHE- 95 | 4.16 | 0 | Hydrophobic |
CEP | CG2 | VAL- 96 | 4.13 | 0 | Hydrophobic |
CAP | CB | VAL- 96 | 4.33 | 0 | Hydrophobic |
O9P | N | VAL- 96 | 2.77 | 166.81 | H-Bond (Protein Donor) |
CAP | CD | ARG- 101 | 3.89 | 0 | Hydrophobic |
O4A | N | GLY- 102 | 3.24 | 158.07 | H-Bond (Protein Donor) |
O1A | N | GLY- 104 | 2.5 | 147.29 | H-Bond (Protein Donor) |
O5A | N | GLY- 106 | 2.71 | 151.13 | H-Bond (Protein Donor) |
O2A | OG | SER- 107 | 2.76 | 151.86 | H-Bond (Protein Donor) |
O2A | N | SER- 107 | 2.71 | 145.93 | H-Bond (Protein Donor) |
CH3 | CB | PHE- 127 | 3.2 | 0 | Hydrophobic |
S1P | CG2 | VAL- 129 | 4.12 | 0 | Hydrophobic |
O5P | ND2 | ASN- 133 | 2.89 | 124.11 | H-Bond (Protein Donor) |
O5P | OG | SER- 136 | 2.77 | 147.87 | H-Bond (Protein Donor) |
C4B | CD1 | PHE- 139 | 4.16 | 0 | Hydrophobic |
C5B | CE1 | PHE- 139 | 3.41 | 0 | Hydrophobic |
CCP | CZ | PHE- 139 | 4.15 | 0 | Hydrophobic |
S1P | CE2 | TYR- 140 | 3.48 | 0 | Hydrophobic |
O7A | CZ | ARG- 142 | 3.09 | 0 | Ionic (Protein Cationic) |
O7A | NH1 | ARG- 143 | 3.26 | 171.55 | H-Bond (Protein Donor) |
O5A | O | HOH- 202 | 2.72 | 179.97 | H-Bond (Protein Donor) |