1.900 Å
X-ray
2011-05-30
Name: | Beta-transaminase |
---|---|
ID: | A3EYF7_9RHIZ |
AC: | A3EYF7 |
Organism: | Mesorhizobium sp. LUK |
Reign: | Bacteria |
TaxID: | 398267 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 21 % |
B | 79 % |
B-Factor: | 16.031 |
---|---|
Number of residues: | 42 |
Including | |
Standard Amino Acids: | 39 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.082 | 1218.375 |
% Hydrophobic | % Polar |
---|---|
39.06 | 60.94 |
According to VolSite |
HET Code: | IK2 |
---|---|
Formula: | C10H12N2O8P |
Molecular weight: | 319.185 g/mol |
DrugBank ID: | DB02783 |
Buried Surface Area: | 75.93 % |
Polar Surface area: | 176.73 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 10 |
H-Bond Donors: | 2 |
Rings: | 1 |
Aromatic rings: | 1 |
Anionic atoms: | 3 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
36.3578 | 81.6532 | 23.0568 |
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 |
O1' | CZ | ARG- 54 | 3.68 | 0 | Ionic (Protein Cationic) |
O2' | CZ | ARG- 54 | 3.73 | 0 | Ionic (Protein Cationic) |
O1' | NE | ARG- 54 | 2.81 | 163.83 | H-Bond (Protein Donor) |
O2' | NH2 | ARG- 54 | 2.94 | 167.58 | H-Bond (Protein Donor) |
O3P | N | GLY- 145 | 3.02 | 155.32 | H-Bond (Protein Donor) |
O1P | N | THR- 146 | 2.87 | 147.55 | H-Bond (Protein Donor) |
O1P | OG1 | THR- 146 | 2.58 | 156.13 | H-Bond (Protein Donor) |
C4A | CE2 | TYR- 172 | 3.77 | 0 | Hydrophobic |
C1' | CE2 | TYR- 172 | 4.28 | 0 | Hydrophobic |
C5A | CE2 | TYR- 172 | 4.2 | 0 | Hydrophobic |
C2A | CG | GLU- 220 | 3.71 | 0 | Hydrophobic |
N1 | OD1 | ASP- 253 | 3.27 | 130.75 | H-Bond (Ligand Donor) |
N1 | OD2 | ASP- 253 | 2.79 | 164.92 | H-Bond (Ligand Donor) |
C2A | CB | VAL- 255 | 4.15 | 0 | Hydrophobic |
C5 | CG1 | VAL- 255 | 3.82 | 0 | Hydrophobic |
OX | NZ | LYS- 280 | 3.02 | 166.99 | H-Bond (Protein Donor) |
O2' | NZ | LYS- 280 | 3.34 | 0 | Ionic (Protein Cationic) |
C1' | CB | ALA- 312 | 3.78 | 0 | Hydrophobic |
O1' | N | GLY- 313 | 2.83 | 160.18 | H-Bond (Protein Donor) |
O2P | OG1 | THR- 314 | 2.9 | 175.97 | H-Bond (Protein Donor) |
O2P | N | THR- 314 | 2.82 | 163.12 | H-Bond (Protein Donor) |
O3P | O | HOH- 2057 | 2.64 | 157.85 | H-Bond (Protein Donor) |