2.350 Å
X-ray
2008-05-08
Name: | Heat shock protein homolog SSE1 |
---|---|
ID: | HSP7F_YEAST |
AC: | P32589 |
Organism: | Saccharomyces cerevisiae |
Reign: | Eukaryota |
TaxID: | 559292 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 92 % |
B | 8 % |
B-Factor: | 33.797 |
---|---|
Number of residues: | 49 |
Including | |
Standard Amino Acids: | 47 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.561 | 972.000 |
% Hydrophobic | % Polar |
---|---|
27.43 | 72.57 |
According to VolSite |
HET Code: | ATP |
---|---|
Formula: | C10H12N5O13P3 |
Molecular weight: | 503.149 g/mol |
DrugBank ID: | DB00171 |
Buried Surface Area: | 75.2 % |
Polar Surface area: | 319.88 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 3 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
86.5515 | 81.7598 | 178.559 |
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 |
O1G | N | ASN- 11 | 2.71 | 152.7 | H-Bond (Protein Donor) |
O1B | N | ASN- 12 | 2.87 | 154.85 | H-Bond (Protein Donor) |
O1B | N | ASN- 13 | 3.05 | 166.86 | H-Bond (Protein Donor) |
O1A | ND2 | ASN- 13 | 3.38 | 133.9 | H-Bond (Protein Donor) |
N6 | O | GLN- 33 | 3.19 | 152.3 | H-Bond (Ligand Donor) |
N6 | OE1 | GLN- 33 | 3.19 | 160.62 | H-Bond (Ligand Donor) |
O1G | NZ | LYS- 69 | 2.86 | 157.2 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 69 | 2.86 | 0 | Ionic (Protein Cationic) |
O3G | NZ | LYS- 69 | 3.81 | 0 | Ionic (Protein Cationic) |
O3B | N | HIS- 206 | 3.04 | 160.82 | H-Bond (Protein Donor) |
O3A | N | HIS- 206 | 3.13 | 130.51 | H-Bond (Protein Donor) |
C4' | CB | HIS- 206 | 4.34 | 0 | Hydrophobic |
O3' | ND1 | HIS- 206 | 3.22 | 131.3 | H-Bond (Ligand Donor) |
O2G | OG | SER- 207 | 2.56 | 162.12 | H-Bond (Protein Donor) |
O2G | N | SER- 207 | 2.89 | 136.72 | H-Bond (Protein Donor) |
O2G | N | SER- 208 | 3.22 | 133.56 | H-Bond (Protein Donor) |
O2' | OE2 | GLU- 272 | 2.77 | 175.63 | H-Bond (Ligand Donor) |
O2' | NZ | LYS- 275 | 2.62 | 160.28 | H-Bond (Protein Donor) |
N1 | OG | SER- 279 | 2.68 | 169.76 | H-Bond (Protein Donor) |
O2A | N | GLY- 343 | 2.95 | 163.64 | H-Bond (Protein Donor) |
O5' | N | GLY- 343 | 3.36 | 133.3 | H-Bond (Protein Donor) |
O4' | OG1 | THR- 344 | 3.41 | 153.9 | H-Bond (Protein Donor) |
N7 | NH1 | ARG- 346 | 2.99 | 148.22 | H-Bond (Protein Donor) |
O3G | MG | MG- 2001 | 2.19 | 0 | Metal Acceptor |
O2B | MG | MG- 2001 | 2.11 | 0 | Metal Acceptor |
N3 | O | HOH- 2060 | 2.96 | 179.96 | H-Bond (Protein Donor) |