2.000 Å
X-ray
1998-03-18
Name: | Peptidyl-prolyl cis-trans isomerase FKBP1A |
---|---|
ID: | FKB1A_HUMAN |
AC: | P62942 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 5.2.1.8 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 35 % |
B | 65 % |
B-Factor: | 17.441 |
---|---|
Number of residues: | 41 |
Including | |
Standard Amino Acids: | 40 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.535 | 486.000 |
% Hydrophobic | % Polar |
---|---|
41.67 | 58.33 |
According to VolSite |
HET Code: | FKA |
---|---|
Formula: | C51H76N2O14 |
Molecular weight: | 941.154 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 49.3 % |
Polar Surface area: | 216.68 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 14 |
H-Bond Donors: | 4 |
Rings: | 5 |
Aromatic rings: | 1 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 11 |
X | Y | Z |
---|---|---|
11.0463 | 11.3208 | 25.6755 |
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 |
C5 | CZ | TYR- 26 | 3.87 | 0 | Hydrophobic |
C35 | CE2 | TYR- 26 | 4.22 | 0 | Hydrophobic |
O6 | OD2 | ASP- 37 | 2.8 | 157.94 | H-Bond (Ligand Donor) |
C16 | CE1 | PHE- 46 | 3.75 | 0 | Hydrophobic |
C35 | CD1 | PHE- 46 | 3.38 | 0 | Hydrophobic |
C36 | CE1 | PHE- 46 | 4.2 | 0 | Hydrophobic |
C40 | CZ | PHE- 46 | 3.38 | 0 | Hydrophobic |
C4 | CE2 | PHE- 46 | 3.59 | 0 | Hydrophobic |
O10 | NE2 | GLN- 53 | 2.87 | 172.3 | H-Bond (Protein Donor) |
C43 | CB | GLU- 54 | 4.04 | 0 | Hydrophobic |
O10 | O | GLU- 54 | 2.77 | 156.77 | H-Bond (Ligand Donor) |
C40 | CG1 | VAL- 55 | 4.5 | 0 | Hydrophobic |
C25 | CG1 | VAL- 55 | 4.48 | 0 | Hydrophobic |
O2 | N | ILE- 56 | 3.05 | 154.83 | H-Bond (Protein Donor) |
C3 | CG1 | ILE- 56 | 4.41 | 0 | Hydrophobic |
C29 | CG2 | ILE- 56 | 3.9 | 0 | Hydrophobic |
C44 | CG2 | ILE- 56 | 3.85 | 0 | Hydrophobic |
C51 | CG2 | ILE- 56 | 4.47 | 0 | Hydrophobic |
C3 | CD2 | TRP- 59 | 3.44 | 0 | Hydrophobic |
C4 | CE2 | TRP- 59 | 3.58 | 0 | Hydrophobic |
C5 | CH2 | TRP- 59 | 4.32 | 0 | Hydrophobic |
C38 | CB | ASP- 79 | 4.43 | 0 | Hydrophobic |
O3 | OH | TYR- 82 | 2.75 | 171.4 | H-Bond (Protein Donor) |
C36 | CE1 | TYR- 82 | 4.11 | 0 | Hydrophobic |
C41 | CZ | TYR- 82 | 4.16 | 0 | Hydrophobic |
C44 | CD1 | TYR- 82 | 3.63 | 0 | Hydrophobic |
C51 | CD1 | TYR- 82 | 3.83 | 0 | Hydrophobic |
C34 | CZ | TYR- 82 | 3.92 | 0 | Hydrophobic |
C29 | CE1 | TYR- 82 | 3.98 | 0 | Hydrophobic |
C11 | CD1 | ILE- 90 | 4.09 | 0 | Hydrophobic |
C34 | CG2 | ILE- 90 | 4.05 | 0 | Hydrophobic |
C34 | CG1 | ILE- 91 | 4.01 | 0 | Hydrophobic |