2.550 Å
X-ray
2012-11-29
Name: | Monoamine oxidase N |
---|---|
ID: | AOFN_ASPNG |
AC: | P46882 |
Organism: | Aspergillus niger |
Reign: | Eukaryota |
TaxID: | 5061 |
EC Number: | 1.4.3.4 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 19.960 |
---|---|
Number of residues: | 74 |
Including | |
Standard Amino Acids: | 67 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 7 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.289 | 1164.375 |
% Hydrophobic | % Polar |
---|---|
53.04 | 46.96 |
According to VolSite |
HET Code: | FAD |
---|---|
Formula: | C27H31N9O15P2 |
Molecular weight: | 783.534 g/mol |
DrugBank ID: | DB03147 |
Buried Surface Area: | 79 % |
Polar Surface area: | 381.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 22 |
H-Bond Donors: | 7 |
Rings: | 6 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
0.0852642 | -21.2847 | 26.9474 |
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 |
O2P | N | CYS- 50 | 2.84 | 162.65 | H-Bond (Protein Donor) |
O3B | OE1 | GLU- 69 | 2.55 | 154.11 | H-Bond (Ligand Donor) |
O2B | OE2 | GLU- 69 | 2.58 | 152.12 | H-Bond (Ligand Donor) |
N3A | N | ALA- 70 | 3.35 | 131.97 | H-Bond (Protein Donor) |
O1A | N | ARG- 77 | 2.76 | 161.96 | H-Bond (Protein Donor) |
O2A | NE | ARG- 77 | 2.53 | 154.17 | H-Bond (Protein Donor) |
O2A | NH2 | ARG- 77 | 3.09 | 127.35 | H-Bond (Protein Donor) |
O3P | NH2 | ARG- 77 | 3.05 | 160.4 | H-Bond (Protein Donor) |
O2A | CZ | ARG- 77 | 3.22 | 0 | Ionic (Protein Cationic) |
C8M | CB | ARG- 77 | 4.28 | 0 | Hydrophobic |
C3' | CB | ARG- 77 | 4 | 0 | Hydrophobic |
O4 | N | THR- 93 | 3.39 | 160.72 | H-Bond (Protein Donor) |
N3 | O | TRP- 94 | 3.03 | 158.71 | H-Bond (Ligand Donor) |
O4 | N | TRP- 94 | 3.09 | 164.17 | H-Bond (Protein Donor) |
N6A | O | VAL- 279 | 3.39 | 166.15 | H-Bond (Ligand Donor) |
N1A | N | VAL- 279 | 2.86 | 174.87 | H-Bond (Protein Donor) |
C5B | CG | PRO- 309 | 4.06 | 0 | Hydrophobic |
C7M | SG | CYS- 338 | 4.33 | 0 | Hydrophobic |
C7M | CD | LYS- 340 | 3.93 | 0 | Hydrophobic |
C8M | CE2 | TRP- 420 | 3.83 | 0 | Hydrophobic |
C2B | CB | PHE- 425 | 4.16 | 0 | Hydrophobic |
C8M | CB | ALA- 429 | 3.31 | 0 | Hydrophobic |
O3P | ND2 | ASN- 456 | 3.23 | 122.48 | H-Bond (Protein Donor) |
O1P | N | SER- 457 | 2.91 | 159.54 | H-Bond (Protein Donor) |
C5' | CB | SER- 457 | 3.78 | 0 | Hydrophobic |
N1 | N | ILE- 467 | 3.46 | 135.62 | H-Bond (Protein Donor) |
O2 | N | ILE- 467 | 2.8 | 166.03 | H-Bond (Protein Donor) |
C2' | CG1 | ILE- 467 | 3.98 | 0 | Hydrophobic |
C5' | CB | ALA- 470 | 3.97 | 0 | Hydrophobic |
O2P | O | HOH- 2010 | 2.89 | 179.99 | H-Bond (Protein Donor) |
O3' | O | HOH- 2020 | 2.85 | 131.23 | H-Bond (Ligand Donor) |
N3 | O | HOH- 2035 | 3.46 | 132.21 | H-Bond (Ligand Donor) |