2.420 Å
X-ray
2003-12-30
Name: | Adenosylmethionine-8-amino-7-oxononanoate aminotransferase |
---|---|
ID: | BIOA_ECOLI |
AC: | P12995 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | 2.6.1.62 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 81 % |
B | 19 % |
B-Factor: | 21.276 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 27 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.930 | 860.625 |
% Hydrophobic | % Polar |
---|---|
50.59 | 49.41 |
According to VolSite |
HET Code: | PLP |
---|---|
Formula: | C8H8NO6P |
Molecular weight: | 245.126 g/mol |
DrugBank ID: | DB00114 |
Buried Surface Area: | 69.05 % |
Polar Surface area: | 132.42 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 1 |
Rings: | 1 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 4 |
X | Y | Z |
---|---|---|
14.4931 | -3.73656 | 20.8458 |
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 |
O1P | OG | SER- 113 | 2.9 | 151.26 | H-Bond (Protein Donor) |
O1P | N | SER- 113 | 3 | 139.3 | H-Bond (Protein Donor) |
C5A | CE2 | TYR- 144 | 4.35 | 0 | Hydrophobic |
C2A | CG | GLU- 211 | 3.89 | 0 | Hydrophobic |
N1 | OD2 | ASP- 245 | 2.92 | 174.21 | H-Bond (Ligand Donor) |
C2A | CB | ILE- 247 | 4.42 | 0 | Hydrophobic |
C5 | CG2 | ILE- 247 | 3.92 | 0 | Hydrophobic |
C2A | CB | ALA- 248 | 4.04 | 0 | Hydrophobic |
C3 | CB | ALA- 248 | 4.21 | 0 | Hydrophobic |
O3 | NZ | LYS- 274 | 2.92 | 136 | H-Bond (Protein Donor) |
DuAr | NZ | LYS- 274 | 3.46 | 125.49 | Pi/Cation |
O4P | OG1 | THR- 309 | 3.39 | 132.59 | H-Bond (Protein Donor) |
O2P | OG1 | THR- 309 | 2.66 | 157.33 | H-Bond (Protein Donor) |
O2P | N | THR- 309 | 3.48 | 134.68 | H-Bond (Protein Donor) |
O3P | OG1 | THR- 309 | 3.12 | 125.31 | H-Bond (Protein Donor) |
O3P | N | THR- 309 | 3.22 | 163.72 | H-Bond (Protein Donor) |
O3 | O | HOH- 566 | 2.75 | 179.95 | H-Bond (Protein Donor) |
O2P | O | HOH- 638 | 3.16 | 179.98 | H-Bond (Protein Donor) |