1.700 Å
X-ray
2007-01-10
Name: | Type A flavoprotein FprA |
---|---|
ID: | FPRA_METTM |
AC: | Q50497 |
Organism: | Methanothermobacter marburgensis |
Reign: | Archaea |
TaxID: | 79929 |
EC Number: | 1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
D | 76 % |
E | 24 % |
B-Factor: | 29.879 |
---|---|
Number of residues: | 38 |
Including | |
Standard Amino Acids: | 36 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 1 |
Cofactors: | |
Metals: | FE |
Ligandability | Volume (Å3) |
---|---|
0.721 | 475.875 |
% Hydrophobic | % Polar |
---|---|
54.61 | 45.39 |
According to VolSite |
HET Code: | FMN |
---|---|
Formula: | C17H19N4O9P |
Molecular weight: | 454.328 g/mol |
DrugBank ID: | DB03247 |
Buried Surface Area: | 82.93 % |
Polar Surface area: | 217.05 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 12 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
13.8593 | 27.2991 | 35.6157 |
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 |
C8M | CZ2 | TRP- 152 | 4.03 | 0 | Hydrophobic |
C1' | CZ2 | TRP- 152 | 3.82 | 0 | Hydrophobic |
C9 | CZ2 | TRP- 152 | 3.29 | 0 | Hydrophobic |
C7M | CD2 | LEU- 202 | 3.6 | 0 | Hydrophobic |
C8M | SD | MET- 266 | 3.83 | 0 | Hydrophobic |
C2' | CE | MET- 266 | 4.08 | 0 | Hydrophobic |
C5' | CE | MET- 266 | 3.96 | 0 | Hydrophobic |
C9 | CE | MET- 266 | 3.83 | 0 | Hydrophobic |
O3P | N | MET- 266 | 2.56 | 147.63 | H-Bond (Protein Donor) |
O1P | N | HIS- 267 | 3.32 | 128.29 | H-Bond (Protein Donor) |
O3P | N | HIS- 267 | 2.66 | 162.29 | H-Bond (Protein Donor) |
O1P | N | SER- 269 | 2.7 | 157.59 | H-Bond (Protein Donor) |
O2P | N | THR- 270 | 2.75 | 165.9 | H-Bond (Protein Donor) |
O2P | OG1 | THR- 270 | 2.62 | 154.21 | H-Bond (Protein Donor) |
C5' | CB | PRO- 316 | 3.51 | 0 | Hydrophobic |
O2' | N | THR- 317 | 3.41 | 130.87 | H-Bond (Protein Donor) |
O2' | O | THR- 317 | 2.69 | 158.67 | H-Bond (Ligand Donor) |
C6 | CG1 | ILE- 318 | 3.69 | 0 | Hydrophobic |
C7M | CD1 | ILE- 318 | 3.33 | 0 | Hydrophobic |
N5 | N | TYR- 319 | 2.88 | 163.19 | H-Bond (Protein Donor) |
C7M | CE2 | TYR- 319 | 3.85 | 0 | Hydrophobic |
O4 | N | ASP- 320 | 2.82 | 140.39 | H-Bond (Protein Donor) |
O4' | OG | SER- 351 | 2.64 | 168.29 | H-Bond (Ligand Donor) |
C4' | CB | SER- 351 | 3.86 | 0 | Hydrophobic |
N1 | N | GLY- 353 | 3.02 | 148.05 | H-Bond (Protein Donor) |
O2 | N | GLY- 353 | 3.06 | 141.93 | H-Bond (Protein Donor) |
O2 | N | GLY- 354 | 2.72 | 132.61 | H-Bond (Protein Donor) |
O2 | N | GLY- 356 | 2.8 | 149.98 | H-Bond (Protein Donor) |
C1' | CE1 | TYR- 381 | 4.36 | 0 | Hydrophobic |
C3' | CE1 | TYR- 381 | 3.71 | 0 | Hydrophobic |
C4' | CD1 | TYR- 381 | 4.23 | 0 | Hydrophobic |