2.230 Å
X-ray
2014-05-30
Name: | KtzI |
---|---|
ID: | A8CF85_9PSEU |
AC: | A8CF85 |
Organism: | Kutzneria sp. 744 |
Reign: | Bacteria |
TaxID: | 345341 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 27.161 |
---|---|
Number of residues: | 59 |
Including | |
Standard Amino Acids: | 50 |
Non Standard Amino Acids: | 2 |
Water Molecules: | 7 |
Cofactors: | NAP |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.988 | 1083.375 |
% Hydrophobic | % Polar |
---|---|
40.50 | 59.50 |
According to VolSite |
HET Code: | FDA |
---|---|
Formula: | C27H33N9O15P2 |
Molecular weight: | 785.550 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 74.74 % |
Polar Surface area: | 381.04 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 21 |
H-Bond Donors: | 9 |
Rings: | 6 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
-48.3493 | 0.171774 | 57.3032 |
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 |
C4' | CG | PRO- 21 | 4.16 | 0 | Hydrophobic |
O2P | N | ALA- 22 | 2.76 | 148.77 | H-Bond (Protein Donor) |
O3B | OE2 | GLU- 43 | 3.14 | 122.33 | H-Bond (Ligand Donor) |
O3B | OE1 | GLU- 43 | 2.64 | 173.08 | H-Bond (Ligand Donor) |
O2B | OE2 | GLU- 43 | 2.75 | 164.72 | H-Bond (Ligand Donor) |
O2B | NE | ARG- 44 | 3.45 | 135.4 | H-Bond (Protein Donor) |
N3A | N | ARG- 44 | 3.3 | 141.04 | H-Bond (Protein Donor) |
C1B | CG | ARG- 44 | 4.34 | 0 | Hydrophobic |
O3' | NE1 | TRP- 50 | 3.16 | 151.33 | H-Bond (Protein Donor) |
O4' | NE1 | TRP- 50 | 3.07 | 127.49 | H-Bond (Protein Donor) |
O4' | NE2 | HIS- 51 | 2.74 | 150.19 | H-Bond (Protein Donor) |
C7M | CB | HIS- 51 | 3.83 | 0 | Hydrophobic |
C7M | CB | MET- 54 | 3.71 | 0 | Hydrophobic |
O4 | N | GLN- 62 | 2.84 | 177.13 | H-Bond (Protein Donor) |
C6 | CD | ARG- 104 | 4.14 | 0 | Hydrophobic |
N6A | O | VAL- 128 | 2.82 | 166.37 | H-Bond (Ligand Donor) |
N1A | N | VAL- 128 | 2.95 | 164.21 | H-Bond (Protein Donor) |
C1' | CD1 | LEU- 166 | 4.32 | 0 | Hydrophobic |
C8M | CZ | TYR- 346 | 3.47 | 0 | Hydrophobic |
O2' | O | SER- 403 | 2.75 | 172.28 | H-Bond (Ligand Donor) |
C1' | CD2 | LEU- 404 | 4.37 | 0 | Hydrophobic |
O2 | N | LEU- 405 | 2.65 | 169.8 | H-Bond (Protein Donor) |
C3' | CD2 | LEU- 405 | 3.87 | 0 | Hydrophobic |
C7M | C5N | NAP- 502 | 3.6 | 0 | Hydrophobic |
C9 | C4D | NAP- 502 | 4.27 | 0 | Hydrophobic |
O1P | O | HOH- 661 | 2.73 | 155.77 | H-Bond (Protein Donor) |