2.400 Å
X-ray
1998-10-26
Name: | 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 4 |
---|---|
ID: | F264_RAT |
AC: | P25114 |
Organism: | Rattus norvegicus |
Reign: | Eukaryota |
TaxID: | 10116 |
EC Number: | 2.7.1.105 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 30.793 |
---|---|
Number of residues: | 40 |
Including | |
Standard Amino Acids: | 37 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 2 |
Cofactors: | |
Metals: | MG |
Ligandability | Volume (Å3) |
---|---|
1.307 | 543.375 |
% Hydrophobic | % Polar |
---|---|
55.28 | 44.72 |
According to VolSite |
HET Code: | ANP |
---|---|
Formula: | C10H13N6O12P3 |
Molecular weight: | 502.164 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 62.29 % |
Polar Surface area: | 322.68 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 16 |
H-Bond Donors: | 4 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 4 |
Cationic atoms: | 0 |
Rule of Five Violation: | 2 |
Rotatable Bonds: | 8 |
X | Y | Z |
---|---|---|
76.2995 | -46.0482 | -41.8436 |
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 | ARG- 49 | 3.07 | 154.51 | H-Bond (Protein Donor) |
O3A | N | GLY- 50 | 3.14 | 140.45 | H-Bond (Protein Donor) |
O2G | NZ | LYS- 51 | 3.23 | 157.88 | H-Bond (Protein Donor) |
O2B | NZ | LYS- 51 | 2.78 | 147.39 | H-Bond (Protein Donor) |
O2B | N | LYS- 51 | 3.19 | 153.21 | H-Bond (Protein Donor) |
O2G | NZ | LYS- 51 | 3.23 | 0 | Ionic (Protein Cationic) |
O2B | NZ | LYS- 51 | 2.78 | 0 | Ionic (Protein Cationic) |
O1B | N | THR- 52 | 2.98 | 146.26 | H-Bond (Protein Donor) |
O2A | N | TYR- 53 | 2.91 | 150.41 | H-Bond (Protein Donor) |
C5' | CB | TYR- 53 | 3.95 | 0 | Hydrophobic |
C2' | CD1 | TYR- 53 | 4.15 | 0 | Hydrophobic |
C4' | CB | ASN- 167 | 4.45 | 0 | Hydrophobic |
N3 | ND2 | ASN- 167 | 3.3 | 128.25 | H-Bond (Protein Donor) |
C3' | CG | GLN- 170 | 4.42 | 0 | Hydrophobic |
C2' | CG1 | VAL- 246 | 4.49 | 0 | Hydrophobic |
C3' | CB | ALA- 426 | 4.27 | 0 | Hydrophobic |
O2A | OH | TYR- 427 | 3.39 | 168.29 | H-Bond (Protein Donor) |
C5' | CE1 | TYR- 427 | 4.4 | 0 | Hydrophobic |
O1G | MG | MG- 501 | 2.5 | 0 | Metal Acceptor |
O1B | MG | MG- 501 | 2.31 | 0 | Metal Acceptor |
N6 | O | HOH- 610 | 3.01 | 136.49 | H-Bond (Ligand Donor) |
N1 | O | HOH- 671 | 3.16 | 179.97 | H-Bond (Protein Donor) |