2.710 Å
X-ray
2005-03-20
Name: | Tubulin gamma-1 chain |
---|---|
ID: | TBG1_HUMAN |
AC: | P23258 |
Organism: | Homo sapiens |
Reign: | Eukaryota |
TaxID: | 9606 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 43.613 |
---|---|
Number of residues: | 38 |
Including | |
Standard Amino Acids: | 37 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.139 | 381.375 |
% Hydrophobic | % Polar |
---|---|
38.05 | 61.95 |
According to VolSite |
HET Code: | GSP |
---|---|
Formula: | C10H14N5O13P3S |
Molecular weight: | 537.230 g/mol |
DrugBank ID: | DB01864 |
Buried Surface Area: | 63.76 % |
Polar Surface area: | 344.91 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 6 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
15.7189 | -11.7287 | 16.6798 |
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 |
O2B | N | GLN- 12 | 2.8 | 141.5 | H-Bond (Protein Donor) |
O1A | N | CYS- 13 | 2.88 | 153.4 | H-Bond (Protein Donor) |
O6 | NE2 | GLN- 16 | 2.71 | 139.21 | H-Bond (Protein Donor) |
O3G | N | ASN- 102 | 3.44 | 124.11 | H-Bond (Protein Donor) |
O3A | OG | SER- 140 | 3.38 | 131.11 | H-Bond (Protein Donor) |
O5' | OG | SER- 140 | 3.19 | 162.51 | H-Bond (Protein Donor) |
C4' | CB | SER- 140 | 3.79 | 0 | Hydrophobic |
C4' | CB | ALA- 142 | 4.05 | 0 | Hydrophobic |
O3G | N | GLY- 144 | 2.7 | 130.25 | H-Bond (Protein Donor) |
O2G | OG1 | THR- 145 | 3.34 | 153.97 | H-Bond (Protein Donor) |
O3G | N | THR- 145 | 3.18 | 149.79 | H-Bond (Protein Donor) |
O1B | N | GLY- 146 | 2.99 | 147.51 | H-Bond (Protein Donor) |
C1' | CG1 | VAL- 171 | 4.35 | 0 | Hydrophobic |
O3' | NE2 | GLN- 184 | 3.48 | 121.41 | H-Bond (Protein Donor) |
O2' | ND2 | ASN- 207 | 3.06 | 120.21 | H-Bond (Protein Donor) |
N3 | ND2 | ASN- 207 | 3.13 | 162.89 | H-Bond (Protein Donor) |
N2 | OD1 | ASN- 207 | 2.95 | 156.88 | H-Bond (Ligand Donor) |
C2' | CZ | PHE- 225 | 3.66 | 0 | Hydrophobic |
O6 | ND2 | ASN- 229 | 2.94 | 174.68 | H-Bond (Protein Donor) |
N1 | OD1 | ASN- 229 | 2.65 | 172.45 | H-Bond (Ligand Donor) |
N2 | OD1 | ASN- 229 | 3.32 | 129.98 | H-Bond (Ligand Donor) |
O2G | MG | MG- 475 | 1.94 | 0 | Metal Acceptor |
O2B | MG | MG- 475 | 2.65 | 0 | Metal Acceptor |