2.900 Å
X-ray
2000-03-02
Name: | Serine hydroxymethyltransferase, cytosolic |
---|---|
ID: | GLYC_MOUSE |
AC: | P50431 |
Organism: | Mus musculus |
Reign: | Eukaryota |
TaxID: | 10090 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 68 % |
B | 32 % |
B-Factor: | 81.026 |
---|---|
Number of residues: | 38 |
Including | |
Standard Amino Acids: | 37 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 0 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.898 | 496.125 |
% Hydrophobic | % Polar |
---|---|
52.38 | 47.62 |
According to VolSite |
HET Code: | THF |
---|---|
Formula: | C20H21N7O7 |
Molecular weight: | 471.423 g/mol |
DrugBank ID: | DB02800 |
Buried Surface Area: | 58.43 % |
Polar Surface area: | 224.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 13 |
H-Bond Donors: | 5 |
Rings: | 3 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 10 |
X | Y | Z |
---|---|---|
109.434 | 71.3457 | 92.1381 |
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 |
N5 | OE1 | GLU- 75 | 3.7 | 0 | Ionic (Ligand Cationic) |
O3 | OE2 | GLU- 75 | 2.93 | 175.26 | H-Bond (Ligand Donor) |
O3 | OE1 | GLU- 75 | 3.44 | 130.75 | H-Bond (Ligand Donor) |
C9 | CD2 | TYR- 82 | 3.68 | 0 | Hydrophobic |
C15 | CE2 | TYR- 82 | 3.33 | 0 | Hydrophobic |
C13 | CD2 | LEU- 143 | 3.88 | 0 | Hydrophobic |
NA2 | O | GLY- 147 | 3.21 | 139.18 | H-Bond (Ligand Donor) |
N3 | O | GLY- 147 | 2.9 | 168 | H-Bond (Ligand Donor) |
O4 | N | LEU- 149 | 3.08 | 152.02 | H-Bond (Protein Donor) |
C15 | CD1 | LEU- 149 | 3.95 | 0 | Hydrophobic |
C16 | CD2 | LEU- 149 | 4.09 | 0 | Hydrophobic |
OE1 | NZ | LYS- 158 | 3.31 | 163.39 | H-Bond (Protein Donor) |
OE1 | NZ | LYS- 158 | 3.31 | 0 | Ionic (Protein Cationic) |
CB | CD1 | ILE- 160 | 4.01 | 0 | Hydrophobic |
C16 | CB | PRO- 298 | 4.06 | 0 | Hydrophobic |
CG | CG | PRO- 298 | 3.96 | 0 | Hydrophobic |
N1 | ND2 | ASN- 387 | 2.63 | 132.64 | H-Bond (Protein Donor) |
C12 | CB | ALA- 395 | 3.4 | 0 | Hydrophobic |