2.310 Å
X-ray
2008-10-02
Name: | Biotin carboxylase |
---|---|
ID: | ACCC_ECOLI |
AC: | P24182 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | 6.3.4.14 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 29.187 |
---|---|
Number of residues: | 29 |
Including | |
Standard Amino Acids: | 28 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.701 | 1161.000 |
% Hydrophobic | % Polar |
---|---|
37.21 | 62.79 |
According to VolSite |
HET Code: | LZL |
---|---|
Formula: | C17H15N5 |
Molecular weight: | 289.334 g/mol |
DrugBank ID: | DB08146 |
Buried Surface Area: | 62.91 % |
Polar Surface area: | 67.93 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 5 |
H-Bond Donors: | 1 |
Rings: | 4 |
Aromatic rings: | 3 |
Anionic atoms: | 0 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 2 |
X | Y | Z |
---|---|---|
4.86091 | -22.7675 | 24.1655 |
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 |
N18 | NZ | LYS- 159 | 2.84 | 145.13 | H-Bond (Protein Donor) |
N6 | NZ | LYS- 159 | 3.17 | 141.03 | H-Bond (Protein Donor) |
C1 | CE | MET- 169 | 4.28 | 0 | Hydrophobic |
N22 | OE2 | GLU- 201 | 3.2 | 158.61 | H-Bond (Ligand Donor) |
N22 | O | LYS- 202 | 2.73 | 158.98 | H-Bond (Ligand Donor) |
N20 | N | LEU- 204 | 3.18 | 164.53 | H-Bond (Protein Donor) |
C19 | CG | GLN- 233 | 3.97 | 0 | Hydrophobic |
C9 | CD1 | LEU- 278 | 3.47 | 0 | Hydrophobic |
C7 | CD2 | LEU- 278 | 4.31 | 0 | Hydrophobic |
C4 | CD2 | LEU- 278 | 3.88 | 0 | Hydrophobic |
C13 | CG2 | ILE- 437 | 3.92 | 0 | Hydrophobic |
C3 | CD1 | ILE- 437 | 3.63 | 0 | Hydrophobic |