2.150 Å
X-ray
2014-03-13
Name: | Neprilysin |
---|---|
ID: | NEP_HUMAN |
AC: | P08473 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 31.159 |
---|---|
Number of residues: | 26 |
Including | |
Standard Amino Acids: | 25 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | ZN |
Ligandability | Volume (Å3) |
---|---|
0.329 | 553.500 |
% Hydrophobic | % Polar |
---|---|
47.56 | 52.44 |
According to VolSite |
HET Code: | RDF |
---|---|
Formula: | C23H32N3O10P |
Molecular weight: | 541.488 g/mol |
DrugBank ID: | DB02557 |
Buried Surface Area: | 55.54 % |
Polar Surface area: | 226.14 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 10 |
H-Bond Donors: | 6 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 11 |
X | Y | Z |
---|---|---|
-51.9896 | -4.23784 | -15.6794 |
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 |
CZ2 | CB | PHE- 106 | 3.49 | 0 | Hydrophobic |
NE1 | O | VAL- 541 | 2.85 | 161.73 | H-Bond (Ligand Donor) |
CZ2 | CG1 | VAL- 541 | 3.84 | 0 | Hydrophobic |
N1 | OD1 | ASN- 542 | 3.33 | 154.03 | H-Bond (Ligand Donor) |
OXT | ND2 | ASN- 542 | 3 | 154.49 | H-Bond (Protein Donor) |
N | O | ALA- 543 | 3.06 | 145.3 | H-Bond (Ligand Donor) |
CB | CB | ALA- 543 | 4.3 | 0 | Hydrophobic |
C2 | CE2 | PHE- 544 | 3.81 | 0 | Hydrophobic |
C3 | CD2 | PHE- 544 | 3.93 | 0 | Hydrophobic |
CD2 | CD1 | ILE- 558 | 3.55 | 0 | Hydrophobic |
CD2 | CE1 | PHE- 563 | 4.33 | 0 | Hydrophobic |
CH2 | CZ | PHE- 563 | 3.48 | 0 | Hydrophobic |
CD1 | CG2 | VAL- 580 | 3.95 | 0 | Hydrophobic |
CD2 | CG2 | VAL- 580 | 3.93 | 0 | Hydrophobic |
CD1 | CB | HIS- 583 | 4.19 | 0 | Hydrophobic |
O1P | OE1 | GLU- 584 | 2.69 | 157.95 | H-Bond (Protein Donor) |
N | OE2 | GLU- 584 | 3.48 | 122.4 | H-Bond (Ligand Donor) |
CB1 | CZ3 | TRP- 693 | 4.34 | 0 | Hydrophobic |
CE3 | CZ3 | TRP- 693 | 3.48 | 0 | Hydrophobic |
CG | CH2 | TRP- 693 | 3.76 | 0 | Hydrophobic |
C6 | CG2 | VAL- 710 | 3.64 | 0 | Hydrophobic |
O2P | NE2 | HIS- 711 | 2.95 | 163.96 | H-Bond (Protein Donor) |
O | NH1 | ARG- 717 | 2.98 | 138.18 | H-Bond (Protein Donor) |
O | NH2 | ARG- 717 | 2.88 | 143.02 | H-Bond (Protein Donor) |
O2P | ZN | ZN- 1750 | 1.96 | 0 | Metal Acceptor |