1.780 Å
X-ray
2006-01-17
Name: | Cystathionine beta-lyase MetC |
---|---|
ID: | METC_ECOLI |
AC: | P06721 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | 4.4.1.8 |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 19.061 |
---|---|
Number of residues: | 35 |
Including | |
Standard Amino Acids: | 33 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.416 | 513.000 |
% Hydrophobic | % Polar |
---|---|
51.97 | 48.03 |
According to VolSite |
HET Code: | P3F |
---|---|
Formula: | C18H16F3N4O7P |
Molecular weight: | 488.311 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 52.93 % |
Polar Surface area: | 185.9 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 9 |
H-Bond Donors: | 3 |
Rings: | 2 |
Aromatic rings: | 2 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 9 |
X | Y | Z |
---|---|---|
-10.1001 | 48.3535 | 26.6156 |
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 |
O3 | N | GLY- 86 | 2.88 | 153.49 | H-Bond (Protein Donor) |
O4 | N | ALA- 87 | 2.81 | 171.67 | H-Bond (Protein Donor) |
C5 | CB | ALA- 87 | 4.4 | 0 | Hydrophobic |
C5 | CE2 | TYR- 111 | 3.38 | 0 | Hydrophobic |
C1 | CB | TYR- 111 | 4.29 | 0 | Hydrophobic |
C17 | CB | TYR- 111 | 4.46 | 0 | Hydrophobic |
N4 | OH | TYR- 111 | 3.01 | 160.61 | H-Bond (Ligand Donor) |
DuAr | DuAr | TYR- 111 | 3.68 | 0 | Aromatic Face/Face |
C13 | CG | PRO- 113 | 3.3 | 0 | Hydrophobic |
C12 | CG | PRO- 113 | 3.36 | 0 | Hydrophobic |
N1 | OD2 | ASP- 185 | 2.71 | 166.31 | H-Bond (Ligand Donor) |
C1 | CB | THR- 187 | 4.31 | 0 | Hydrophobic |
C4 | CB | ALA- 207 | 3.9 | 0 | Hydrophobic |
O3 | OG1 | THR- 209 | 2.75 | 166.39 | H-Bond (Protein Donor) |
O2 | NZ | LYS- 210 | 3.42 | 0 | Ionic (Protein Cationic) |
N2 | NZ | LYS- 210 | 2.81 | 134.64 | H-Bond (Protein Donor) |
F2 | CD2 | TYR- 338 | 3.97 | 0 | Hydrophobic |
F3 | CB | TYR- 338 | 4.47 | 0 | Hydrophobic |
O5 | N | SER- 339 | 3.42 | 143.6 | H-Bond (Protein Donor) |
C1 | CZ2 | TRP- 340 | 4.06 | 0 | Hydrophobic |
O9 | NE1 | TRP- 340 | 2.97 | 149.29 | H-Bond (Protein Donor) |
O5 | NH2 | ARG- 372 | 3.19 | 151.84 | H-Bond (Protein Donor) |
O5 | NH1 | ARG- 372 | 3.34 | 143.3 | H-Bond (Protein Donor) |