2.200 Å
X-ray
2004-07-29
Name: | Gamma-aminobutyraldehyde dehydrogenase |
---|---|
ID: | ABDH_ECOLI |
AC: | P77674 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | 1.2.1.19 |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 13.242 |
---|---|
Number of residues: | 46 |
Including | |
Standard Amino Acids: | 45 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.118 | 567.000 |
% Hydrophobic | % Polar |
---|---|
38.69 | 61.31 |
According to VolSite |
HET Code: | NAI |
---|---|
Formula: | C21H27N7O14P2 |
Molecular weight: | 663.425 g/mol |
DrugBank ID: | DB00157 |
Buried Surface Area: | 67.47 % |
Polar Surface area: | 342.9 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 19 |
H-Bond Donors: | 6 |
Rings: | 5 |
Aromatic rings: | 2 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 11 |
X | Y | Z |
---|---|---|
51.0871 | 29.3057 | 58.4592 |
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 |
C1B | CG2 | ILE- 145 | 3.39 | 0 | Hydrophobic |
O3B | O | ALA- 146 | 2.72 | 176.38 | H-Bond (Ligand Donor) |
C5B | CB | PRO- 147 | 4.34 | 0 | Hydrophobic |
C4N | CB | PRO- 147 | 3.64 | 0 | Hydrophobic |
O1N | NE1 | TRP- 148 | 2.77 | 167.13 | H-Bond (Protein Donor) |
O2B | NZ | LYS- 172 | 2.8 | 172.22 | H-Bond (Protein Donor) |
C3B | CB | SER- 174 | 4.09 | 0 | Hydrophobic |
O2B | OE1 | GLU- 175 | 3.06 | 147.49 | H-Bond (Ligand Donor) |
N6A | OD1 | ASP- 209 | 2.91 | 151.74 | H-Bond (Ligand Donor) |
C4B | CD1 | LEU- 222 | 4.06 | 0 | Hydrophobic |
O1A | OG | SER- 225 | 3.25 | 150.94 | H-Bond (Protein Donor) |
O1A | N | SER- 225 | 2.93 | 178.45 | H-Bond (Protein Donor) |
C1D | CB | SER- 225 | 3.65 | 0 | Hydrophobic |
C4D | CB | SER- 225 | 3.8 | 0 | Hydrophobic |
O1A | OG1 | THR- 228 | 2.54 | 141.52 | H-Bond (Protein Donor) |
O2A | OG1 | THR- 228 | 3.12 | 125.3 | H-Bond (Protein Donor) |
C1B | CG2 | THR- 228 | 4.23 | 0 | Hydrophobic |
N7N | OE1 | GLU- 246 | 3.34 | 133.26 | H-Bond (Ligand Donor) |
O2D | OE1 | GLU- 378 | 2.62 | 162.84 | H-Bond (Ligand Donor) |
C3D | CD2 | PHE- 380 | 4.16 | 0 | Hydrophobic |
C2D | CG | PHE- 380 | 3.9 | 0 | Hydrophobic |
C4N | CZ | PHE- 380 | 3.91 | 0 | Hydrophobic |