2.200 Å
X-ray
2013-12-18
Name: | Tubulin alpha-1B chain |
---|---|
ID: | TBA1B_BOVIN |
AC: | P81947 |
Organism: | Bos taurus |
Reign: | Eukaryota |
TaxID: | 9913 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
C | 96 % |
D | 4 % |
B-Factor: | 36.951 |
---|---|
Number of residues: | 50 |
Including | |
Standard Amino Acids: | 45 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 4 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
0.800 | 901.125 |
% Hydrophobic | % Polar |
---|---|
41.95 | 58.05 |
According to VolSite |
HET Code: | GTP |
---|---|
Formula: | C10H12N5O14P3 |
Molecular weight: | 519.149 g/mol |
DrugBank ID: | DB04137 |
Buried Surface Area: | 83.14 % |
Polar Surface area: | 335.56 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 17 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
14.9984 | 19.5914 | -13.9104 |
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 |
O1B | N | GLN- 11 | 3.1 | 177.09 | H-Bond (Protein Donor) |
N7 | NE2 | GLN- 11 | 3.12 | 154.93 | H-Bond (Protein Donor) |
O2A | N | ALA- 12 | 3.05 | 168.15 | H-Bond (Protein Donor) |
C1' | CB | ALA- 12 | 4.28 | 0 | Hydrophobic |
O6 | NE2 | GLN- 15 | 2.75 | 149.65 | H-Bond (Protein Donor) |
O3G | N | ALA- 99 | 2.94 | 161.08 | H-Bond (Protein Donor) |
O2G | N | ASN- 101 | 2.74 | 155.12 | H-Bond (Protein Donor) |
O5' | OG | SER- 140 | 2.97 | 171.96 | H-Bond (Protein Donor) |
C1' | CB | SER- 140 | 4.39 | 0 | Hydrophobic |
C4' | CB | SER- 140 | 3.91 | 0 | Hydrophobic |
O2G | N | GLY- 144 | 3.09 | 147.34 | H-Bond (Protein Donor) |
O3G | OG1 | THR- 145 | 2.81 | 168.02 | H-Bond (Protein Donor) |
O3B | N | THR- 145 | 2.94 | 167.51 | H-Bond (Protein Donor) |
O2B | N | GLY- 146 | 2.95 | 139.55 | H-Bond (Protein Donor) |
C1' | CG2 | ILE- 171 | 4.43 | 0 | Hydrophobic |
O2' | O | VAL- 177 | 2.6 | 145.38 | H-Bond (Ligand Donor) |
C3' | CG2 | THR- 179 | 3.69 | 0 | Hydrophobic |
O3' | OE1 | GLU- 183 | 3.34 | 139.13 | H-Bond (Ligand Donor) |
O3' | OE2 | GLU- 183 | 2.72 | 158.59 | H-Bond (Ligand Donor) |
O2' | ND2 | ASN- 206 | 3.25 | 123.31 | H-Bond (Protein Donor) |
N3 | ND2 | ASN- 206 | 3.04 | 172.2 | H-Bond (Protein Donor) |
N2 | OD1 | ASN- 206 | 2.76 | 149 | H-Bond (Ligand Donor) |
O2' | OH | TYR- 224 | 3.09 | 150.57 | H-Bond (Protein Donor) |
DuAr | DuAr | TYR- 224 | 3.76 | 0 | Aromatic Face/Face |
C2' | CZ | TYR- 224 | 4.07 | 0 | Hydrophobic |
O6 | ND2 | ASN- 228 | 3.09 | 163.14 | H-Bond (Protein Donor) |
N1 | OD1 | ASN- 228 | 2.66 | 173.64 | H-Bond (Ligand Donor) |
O1G | NZ | LYS- 254 | 2.86 | 166.25 | H-Bond (Protein Donor) |
O1G | NZ | LYS- 254 | 2.86 | 0 | Ionic (Protein Cationic) |
O2G | NZ | LYS- 254 | 3.89 | 0 | Ionic (Protein Cationic) |
O1G | MG | MG- 502 | 2.11 | 0 | Metal Acceptor |
O1B | MG | MG- 502 | 2.16 | 0 | Metal Acceptor |
O3' | O | HOH- 613 | 2.73 | 179.99 | H-Bond (Protein Donor) |
O3' | O | HOH- 626 | 3.34 | 179.97 | H-Bond (Protein Donor) |