1.350 Å
X-ray
2011-03-25
Name: | MccE protein |
---|---|
ID: | Q47510_ECOLX |
AC: | Q47510 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 562 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 12.975 |
---|---|
Number of residues: | 37 |
Including | |
Standard Amino Acids: | 35 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | COA |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.693 | 594.000 |
% Hydrophobic | % Polar |
---|---|
47.16 | 52.84 |
According to VolSite |
HET Code: | 7MC |
---|---|
Formula: | C19H29N8O10P |
Molecular weight: | 560.455 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 59.91 % |
Polar Surface area: | 290.62 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 14 |
H-Bond Donors: | 6 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 1 |
Cationic atoms: | 1 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
64.4752 | 7.90647 | 7.41416 |
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 |
C5' | SD | MET- 46 | 3.92 | 0 | Hydrophobic |
C1' | CZ2 | TRP- 48 | 4.17 | 0 | Hydrophobic |
O1P | NE1 | TRP- 48 | 2.87 | 127.58 | H-Bond (Protein Donor) |
DuAr | DuAr | TRP- 48 | 3.51 | 0 | Aromatic Face/Face |
DuAr | DuAr | PHE- 61 | 3.48 | 0 | Aromatic Face/Face |
C1' | CG1 | VAL- 88 | 4.09 | 0 | Hydrophobic |
O2' | OG | SER- 90 | 3.44 | 155.79 | H-Bond (Ligand Donor) |
O3' | OG | SER- 90 | 2.78 | 157.81 | H-Bond (Ligand Donor) |
C3' | CB | SER- 90 | 4.24 | 0 | Hydrophobic |
O | ND2 | ASN- 92 | 2.83 | 143.04 | H-Bond (Protein Donor) |
C37 | CD1 | TYR- 105 | 4.49 | 0 | Hydrophobic |
N3 | NE1 | TRP- 106 | 3.08 | 169.62 | H-Bond (Protein Donor) |
N | O | LYS- 140 | 2.84 | 134.57 | H-Bond (Ligand Donor) |
OD1 | NE2 | GLN- 176 | 3.3 | 152.74 | H-Bond (Protein Donor) |
N8 | O | HOH- 205 | 2.8 | 174.42 | H-Bond (Ligand Donor) |
C37 | C2P | COA- 400 | 3.33 | 0 | Hydrophobic |