2.150 Å
X-ray
2010-11-17
Min | Mean | Median | Standard Deviation | Max | Count | |
---|---|---|---|---|---|---|
pChEMBL: | 6.820 | 8.370 | 8.400 | 0.840 | 9.190 | 7 |
Name: | Angiotensin-converting enzyme |
---|---|
ID: | ACE_HUMAN |
AC: | P12821 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 3.2.1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 26.534 |
---|---|
Number of residues: | 51 |
Including | |
Standard Amino Acids: | 47 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 3 |
Cofactors: | |
Metals: | ZN |
Ligandability | Volume (Å3) |
---|---|
0.222 | 2544.750 |
% Hydrophobic | % Polar |
---|---|
34.75 | 65.25 |
According to VolSite |
HET Code: | 3ES |
---|---|
Formula: | C38H36N3O9P |
Molecular weight: | 709.681 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 60.79 % |
Polar Surface area: | 203.76 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 9 |
H-Bond Donors: | 3 |
Rings: | 5 |
Aromatic rings: | 5 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 17 |
X | Y | Z |
---|---|---|
1.62871 | -16.4594 | -21.8925 |
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 |
O | NE2 | GLN- 259 | 3 | 154.12 | H-Bond (Protein Donor) |
CAJ | CB | SER- 260 | 4.47 | 0 | Hydrophobic |
OAC | NE2 | HIS- 331 | 2.64 | 171.34 | H-Bond (Protein Donor) |
CBF | CB | ALA- 332 | 4.39 | 0 | Hydrophobic |
CAS | CB | SER- 333 | 3.72 | 0 | Hydrophobic |
OAB | N | ALA- 334 | 2.76 | 175.72 | H-Bond (Protein Donor) |
CAJ | CB | ASP- 354 | 3.97 | 0 | Hydrophobic |
CBB | CB | HIS- 365 | 4.29 | 0 | Hydrophobic |
DuAr | DuAr | HIS- 388 | 3.77 | 0 | Aromatic Face/Face |
CAK | CB | HIS- 388 | 3.53 | 0 | Hydrophobic |
OH | OD2 | ASP- 393 | 3.25 | 143.33 | H-Bond (Ligand Donor) |
CB | CZ | PHE- 435 | 3.86 | 0 | Hydrophobic |
OXT | NZ | LYS- 489 | 3.79 | 0 | Ionic (Protein Cationic) |
O | NZ | LYS- 489 | 2.62 | 0 | Ionic (Protein Cationic) |
O | NZ | LYS- 489 | 2.62 | 166.69 | H-Bond (Protein Donor) |
CAN | CG2 | THR- 496 | 3.73 | 0 | Hydrophobic |
O | OH | TYR- 498 | 2.58 | 152.6 | H-Bond (Protein Donor) |
CB | CZ | TYR- 498 | 4.11 | 0 | Hydrophobic |
OAD | OH | TYR- 501 | 2.53 | 161.89 | H-Bond (Protein Donor) |
CB | CD1 | TYR- 501 | 3.61 | 0 | Hydrophobic |
CD2 | CD1 | TYR- 501 | 3.46 | 0 | Hydrophobic |
OAG | ZN | ZN- 1620 | 2.34 | 0 | Metal Acceptor |
OAD | ZN | ZN- 1620 | 2.23 | 0 | Metal Acceptor |