2.100 Å
X-ray
2011-04-12
Name: | Cytosolic 10-formyltetrahydrofolate dehydrogenase |
---|---|
ID: | AL1L1_RAT |
AC: | P28037 |
Organism: | Rattus norvegicus |
Reign: | Eukaryota |
TaxID: | 10116 |
EC Number: | 1.5.1.6 |
Chain Name: | Percentage of Residues within binding site |
---|---|
C | 100 % |
B-Factor: | 18.745 |
---|---|
Number of residues: | 58 |
Including | |
Standard Amino Acids: | 55 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.452 | 529.875 |
% Hydrophobic | % Polar |
---|---|
49.04 | 50.96 |
According to VolSite |
HET Code: | NAP |
---|---|
Formula: | C21H25N7O17P3 |
Molecular weight: | 740.381 g/mol |
DrugBank ID: | DB03461 |
Buried Surface Area: | 67.63 % |
Polar Surface area: | 405.54 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 21 |
H-Bond Donors: | 5 |
Rings: | 5 |
Aromatic rings: | 3 |
Anionic atoms: | 4 |
Cationic atoms: | 1 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
86.9748 | 16.5531 | 69.5827 |
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 |
C1B | CG1 | VAL- 570 | 3.65 | 0 | Hydrophobic |
C4B | CG1 | VAL- 570 | 3.7 | 0 | Hydrophobic |
O3B | O | ILE- 571 | 2.78 | 174.28 | H-Bond (Ligand Donor) |
C5B | CB | PRO- 572 | 4.26 | 0 | Hydrophobic |
C5N | CG | PRO- 572 | 3.58 | 0 | Hydrophobic |
O2N | NE1 | TRP- 573 | 2.63 | 136.02 | H-Bond (Protein Donor) |
C5D | CZ2 | TRP- 573 | 4.4 | 0 | Hydrophobic |
C4N | SD | MET- 579 | 3.92 | 0 | Hydrophobic |
O2B | NZ | LYS- 597 | 2.99 | 167.81 | H-Bond (Protein Donor) |
O2X | NZ | LYS- 597 | 2.92 | 0 | Ionic (Protein Cationic) |
O2X | N | GLN- 600 | 2.72 | 172.58 | H-Bond (Protein Donor) |
O3X | N | GLY- 630 | 2.82 | 175.73 | H-Bond (Protein Donor) |
N6A | OE1 | GLN- 635 | 3.19 | 163.68 | H-Bond (Ligand Donor) |
C1B | CE1 | PHE- 648 | 4.36 | 0 | Hydrophobic |
C4B | CE1 | PHE- 648 | 3.81 | 0 | Hydrophobic |
C5N | CG2 | THR- 649 | 3.57 | 0 | Hydrophobic |
O1A | N | SER- 651 | 2.81 | 162.35 | H-Bond (Protein Donor) |
O1A | OG | SER- 651 | 2.74 | 156.75 | H-Bond (Protein Donor) |
O3 | N | SER- 651 | 3.36 | 129.98 | H-Bond (Protein Donor) |
C4D | CB | SER- 651 | 4.23 | 0 | Hydrophobic |
C1B | CG1 | VAL- 654 | 4.3 | 0 | Hydrophobic |
N7N | O | LEU- 674 | 2.86 | 161.62 | H-Bond (Ligand Donor) |
C2D | CB | ALA- 707 | 4.18 | 0 | Hydrophobic |
C4N | CB | ALA- 707 | 3.46 | 0 | Hydrophobic |
O3D | OE1 | GLU- 804 | 2.78 | 164.57 | H-Bond (Ligand Donor) |
O2D | OE2 | GLU- 804 | 2.67 | 156.75 | H-Bond (Ligand Donor) |
O2D | OE1 | GLU- 804 | 3.19 | 122.73 | H-Bond (Ligand Donor) |
C5D | CE2 | PHE- 806 | 3.77 | 0 | Hydrophobic |
C3D | CD1 | PHE- 806 | 4.13 | 0 | Hydrophobic |
C2D | CE1 | PHE- 806 | 3.49 | 0 | Hydrophobic |