2.610 Å
X-ray
2011-07-15
Name: | Ferrous iron transport protein B |
---|---|
ID: | Q5M586_STRT2 |
AC: | Q5M586 |
Organism: | Streptococcus thermophilus |
Reign: | Bacteria |
TaxID: | 264199 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
B | 100 % |
B-Factor: | 20.523 |
---|---|
Number of residues: | 37 |
Including | |
Standard Amino Acids: | 36 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.715 | 411.750 |
% Hydrophobic | % Polar |
---|---|
47.54 | 52.46 |
According to VolSite |
HET Code: | GNP |
---|---|
Formula: | C10H13N6O13P3 |
Molecular weight: | 518.164 g/mol |
DrugBank ID: | DB02082 |
Buried Surface Area: | 74.28 % |
Polar Surface area: | 338.36 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 16 |
H-Bond Donors: | 5 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
-32.3474 | 19.3426 | -46.6078 |
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 |
O1B | N | SER- 12 | 3.3 | 141.69 | H-Bond (Protein Donor) |
O1B | N | GLY- 13 | 3.13 | 142.51 | H-Bond (Protein Donor) |
O3A | N | GLY- 13 | 3.01 | 131.88 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 14 | 2.75 | 149.76 | H-Bond (Protein Donor) |
O1B | N | LYS- 14 | 3.11 | 166.97 | H-Bond (Protein Donor) |
O1B | NZ | LYS- 14 | 2.71 | 137.51 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 14 | 2.75 | 0 | Ionic (Protein Cationic) |
O1B | NZ | LYS- 14 | 2.71 | 0 | Ionic (Protein Cationic) |
O2B | N | THR- 15 | 3.18 | 162.51 | H-Bond (Protein Donor) |
O1A | N | SER- 16 | 2.97 | 141.15 | H-Bond (Protein Donor) |
O1A | OG | SER- 16 | 2.7 | 169.96 | H-Bond (Protein Donor) |
C2' | CG1 | VAL- 28 | 3.76 | 0 | Hydrophobic |
O2A | N | GLY- 29 | 3.28 | 159.58 | H-Bond (Protein Donor) |
C3' | CB | ASN- 30 | 4.33 | 0 | Hydrophobic |
O2G | N | GLY- 33 | 2.79 | 127.49 | H-Bond (Protein Donor) |
O2G | N | VAL- 34 | 2.76 | 143.88 | H-Bond (Protein Donor) |
O3G | N | THR- 35 | 2.83 | 161.71 | H-Bond (Protein Donor) |
N7 | ND2 | ASN- 113 | 3.29 | 136.25 | H-Bond (Protein Donor) |
C4' | CE | MET- 114 | 4.46 | 0 | Hydrophobic |
C1' | CE | MET- 114 | 4.17 | 0 | Hydrophobic |
O6 | N | MET- 114 | 3.35 | 128.45 | H-Bond (Protein Donor) |
N1 | OD1 | ASP- 116 | 2.64 | 164.85 | H-Bond (Ligand Donor) |
N1 | OD2 | ASP- 116 | 3.33 | 128.55 | H-Bond (Ligand Donor) |
N2 | OD2 | ASP- 116 | 2.77 | 157.32 | H-Bond (Ligand Donor) |
O6 | OG | SER- 142 | 3.43 | 160.66 | H-Bond (Protein Donor) |
O6 | N | ALA- 143 | 2.78 | 151.78 | H-Bond (Protein Donor) |
O3G | MG | MG- 301 | 1.97 | 0 | Metal Acceptor |
O2B | MG | MG- 301 | 1.94 | 0 | Metal Acceptor |