2.500 Å
X-ray
1995-02-22
Name: | Aspartate aminotransferase |
---|---|
ID: | AAT_ECOLI |
AC: | P00509 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | 2.6.1.1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 14 % |
B | 86 % |
B-Factor: | 25.251 |
---|---|
Number of residues: | 45 |
Including | |
Standard Amino Acids: | 44 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.013 | 354.375 |
% Hydrophobic | % Polar |
---|---|
40.95 | 59.05 |
According to VolSite |
HET Code: | TYR_PLP |
---|---|
Formula: | C17H19N2O8P |
Molecular weight: | 410.315 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 79.54 % |
Polar Surface area: | 192.31 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 9 |
H-Bond Donors: | 3 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 3 |
Cationic atoms: | 1 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 9 |
X | Y | Z |
---|---|---|
7.31946 | 29.4215 | 24.745 |
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 |
OH | OD2 | ASP- 15 | 2.62 | 144.55 | H-Bond (Ligand Donor) |
CD1 | CG2 | ILE- 17 | 3.7 | 0 | Hydrophobic |
CE1 | CB | ILE- 17 | 3.89 | 0 | Hydrophobic |
CZ | CD1 | LEU- 18 | 3.59 | 0 | Hydrophobic |
CB | CG1 | ILE- 37 | 4.04 | 0 | Hydrophobic |
OXT | N | GLY- 38 | 3.47 | 171.02 | H-Bond (Protein Donor) |
CB | CE2 | TYR- 70 | 3.67 | 0 | Hydrophobic |
O1P | N | GLY- 108 | 2.93 | 172.04 | H-Bond (Protein Donor) |
O3P | N | GLY- 108 | 3.22 | 120.52 | H-Bond (Protein Donor) |
C5A | CB | SER- 109 | 4.29 | 0 | Hydrophobic |
O3P | N | SER- 109 | 2.9 | 139.37 | H-Bond (Protein Donor) |
O3P | OG | SER- 109 | 2.75 | 149.95 | H-Bond (Protein Donor) |
C2A | CB | TRP- 140 | 4.24 | 0 | Hydrophobic |
C4A | CZ2 | TRP- 140 | 3.69 | 0 | Hydrophobic |
C5A | CH2 | TRP- 140 | 3.31 | 0 | Hydrophobic |
DuAr | DuAr | TRP- 140 | 3.55 | 0 | Aromatic Face/Face |
C2A | CB | ASN- 194 | 4.16 | 0 | Hydrophobic |
O3 | ND2 | ASN- 194 | 2.78 | 125.98 | H-Bond (Protein Donor) |
O | ND2 | ASN- 194 | 3.43 | 139.6 | H-Bond (Protein Donor) |
C2A | CE1 | TYR- 225 | 4.3 | 0 | Hydrophobic |
O3 | OH | TYR- 225 | 3.32 | 142.93 | H-Bond (Protein Donor) |
O1P | OG | SER- 255 | 2.55 | 142.62 | H-Bond (Protein Donor) |
O1P | OG | SER- 257 | 3.29 | 161.96 | H-Bond (Protein Donor) |
O2P | NH1 | ARG- 266 | 3.19 | 158.83 | H-Bond (Protein Donor) |
O2P | NH2 | ARG- 266 | 3.39 | 146.61 | H-Bond (Protein Donor) |
O3P | NH2 | ARG- 266 | 2.73 | 137.79 | H-Bond (Protein Donor) |
O2P | CZ | ARG- 266 | 3.78 | 0 | Ionic (Protein Cationic) |
O3P | CZ | ARG- 266 | 3.67 | 0 | Ionic (Protein Cationic) |
CE2 | CB | SER- 296 | 4.37 | 0 | Hydrophobic |
O | NH1 | ARG- 386 | 2.67 | 140.61 | H-Bond (Protein Donor) |
O | NH2 | ARG- 386 | 3.39 | 121.18 | H-Bond (Protein Donor) |
OXT | NH2 | ARG- 386 | 3.34 | 156.92 | H-Bond (Protein Donor) |
O | CZ | ARG- 386 | 3.42 | 0 | Ionic (Protein Cationic) |