2.100 Å
X-ray
2001-08-07
Name: | Insulin-like growth factor 1 receptor |
---|---|
ID: | IGF1R_HUMAN |
AC: | P08069 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | 2.7.10.1 |
Chain Name: | Percentage of Residues within binding site |
---|---|
C | 100 % |
B-Factor: | 40.295 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 29 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.936 | 776.250 |
% Hydrophobic | % Polar |
---|---|
46.09 | 53.91 |
According to VolSite |
HET Code: | ANP |
---|---|
Formula: | C10H13N6O12P3 |
Molecular weight: | 502.164 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 47.74 % |
Polar Surface area: | 322.68 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 16 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
6.28535 | 43.6324 | -7.23732 |
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 |
C1' | CB | LEU- 1005 | 4.4 | 0 | Hydrophobic |
O2B | N | SER- 1009 | 2.72 | 138.13 | H-Bond (Protein Donor) |
C1' | CG1 | VAL- 1013 | 4.19 | 0 | Hydrophobic |
C5' | CG2 | VAL- 1013 | 3.78 | 0 | Hydrophobic |
O1B | NZ | LYS- 1033 | 2.53 | 120.78 | H-Bond (Protein Donor) |
O1B | NZ | LYS- 1033 | 2.53 | 0 | Ionic (Protein Cationic) |
N6 | O | GLU- 1080 | 2.77 | 152.85 | H-Bond (Ligand Donor) |
N1 | N | MET- 1082 | 2.82 | 154.19 | H-Bond (Protein Donor) |
O3G | NZ | LYS- 1171 | 3.71 | 0 | Ionic (Protein Cationic) |