2.000 Å
X-ray
2004-12-08
Name: | GTP cyclohydrolase 1 |
---|---|
ID: | Q5SH52_THET8 |
AC: | Q5SH52 |
Organism: | Thermus thermophilus |
Reign: | Bacteria |
TaxID: | 300852 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 47 % |
E | 53 % |
B-Factor: | 27.793 |
---|---|
Number of residues: | 37 |
Including | |
Standard Amino Acids: | 33 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 3 |
Cofactors: | |
Metals: | ZN |
Ligandability | Volume (Å3) |
---|---|
0.158 | 307.125 |
% Hydrophobic | % Polar |
---|---|
54.95 | 45.05 |
According to VolSite |
HET Code: | 8GT |
---|---|
Formula: | C10H12N5O15P3 |
Molecular weight: | 535.148 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 64.2 % |
Polar Surface area: | 350.08 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 5 |
Rings: | 3 |
Aromatic rings: | 0 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
7.57264 | -29.2509 | 13.9813 |
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' | CB | ALA- 87 | 4.15 | 0 | Hydrophobic |
C4' | CZ | PHE- 89 | 4.07 | 0 | Hydrophobic |
C5' | CB | HIS- 110 | 4.39 | 0 | Hydrophobic |
O1B | NE2 | HIS- 111 | 2.54 | 164.1 | H-Bond (Protein Donor) |
N2 | O | LEU- 130 | 3.16 | 153.44 | H-Bond (Ligand Donor) |
O1G | OG | SER- 133 | 3.26 | 131.05 | H-Bond (Protein Donor) |
O3G | OG | SER- 133 | 2.54 | 157.45 | H-Bond (Protein Donor) |
O2' | N | SER- 133 | 2.76 | 163.88 | H-Bond (Protein Donor) |
O3' | OG | SER- 133 | 2.53 | 153.38 | H-Bond (Ligand Donor) |
C3' | CB | SER- 133 | 4.12 | 0 | Hydrophobic |
O3G | NZ | LYS- 134 | 2.92 | 159.6 | H-Bond (Protein Donor) |
O2A | NZ | LYS- 134 | 3.1 | 148.77 | H-Bond (Protein Donor) |
O3G | NZ | LYS- 134 | 2.92 | 0 | Ionic (Protein Cationic) |
O2A | NZ | LYS- 134 | 3.1 | 0 | Ionic (Protein Cationic) |
O2G | NH2 | ARG- 137 | 2.84 | 159.12 | H-Bond (Protein Donor) |
O3G | NH2 | ARG- 137 | 3.42 | 133.64 | H-Bond (Protein Donor) |
O3G | NE | ARG- 137 | 2.89 | 161.95 | H-Bond (Protein Donor) |
O2G | CZ | ARG- 137 | 3.8 | 0 | Ionic (Protein Cationic) |
O3G | CZ | ARG- 137 | 3.6 | 0 | Ionic (Protein Cationic) |
O6 | N | GLN- 149 | 2.7 | 168.06 | H-Bond (Protein Donor) |
N1 | OE1 | GLU- 150 | 2.84 | 168.22 | H-Bond (Protein Donor) |
N2 | OE2 | GLU- 150 | 2.6 | 153.89 | H-Bond (Ligand Donor) |
N2 | OE1 | GLU- 150 | 3.31 | 138.15 | H-Bond (Ligand Donor) |
O1G | NH2 | ARG- 183 | 3.46 | 132.36 | H-Bond (Protein Donor) |
O1G | NH1 | ARG- 183 | 2.83 | 170.94 | H-Bond (Protein Donor) |
O2G | NH2 | ARG- 183 | 2.81 | 160.71 | H-Bond (Protein Donor) |
O1G | CZ | ARG- 183 | 3.59 | 0 | Ionic (Protein Cationic) |
O2G | CZ | ARG- 183 | 3.8 | 0 | Ionic (Protein Cationic) |
O1B | CZ | ARG- 183 | 3.86 | 0 | Ionic (Protein Cationic) |
O8 | ZN | ZN- 1005 | 2.02 | 0 | Metal Acceptor |
O1G | O | HOH- 1013 | 2.88 | 158.31 | H-Bond (Protein Donor) |