2.200 Å
X-ray
2010-01-15
Name: | Subunit alpha of sarocosine oxidase |
---|---|
ID: | Q50LF0_9CORY |
AC: | Q50LF0 |
Organism: | Corynebacterium sp. U-96 |
Reign: | Bacteria |
TaxID: | 31944 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 23.701 |
---|---|
Number of residues: | 56 |
Including | |
Standard Amino Acids: | 51 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 5 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.284 | 928.125 |
% Hydrophobic | % Polar |
---|---|
52.36 | 47.64 |
According to VolSite |
HET Code: | NAD |
---|---|
Formula: | C21H26N7O14P2 |
Molecular weight: | 662.417 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 70.1 % |
Polar Surface area: | 343.54 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 18 |
H-Bond Donors: | 6 |
Rings: | 5 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 1 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 11 |
X | Y | Z |
---|---|---|
-31.7467 | 115.583 | 22.2134 |
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 |
C3D | CG | PRO- 137 | 3.88 | 0 | Hydrophobic |
C4D | CG | PRO- 137 | 3.89 | 0 | Hydrophobic |
O2N | N | ALA- 138 | 2.98 | 157.79 | H-Bond (Protein Donor) |
O3B | OD2 | ASP- 157 | 3.48 | 122.88 | H-Bond (Ligand Donor) |
O3B | OD1 | ASP- 157 | 2.7 | 168.93 | H-Bond (Ligand Donor) |
O2B | OE2 | GLU- 158 | 2.62 | 167.54 | H-Bond (Ligand Donor) |
N3A | N | GLU- 158 | 3.15 | 142.67 | H-Bond (Protein Donor) |
C1B | CG | GLU- 158 | 4.2 | 0 | Hydrophobic |
O2B | NE | ARG- 159 | 2.94 | 159.26 | H-Bond (Protein Donor) |
O1A | N | THR- 165 | 2.85 | 166.61 | H-Bond (Protein Donor) |
O1A | OG1 | THR- 165 | 3.16 | 143.1 | H-Bond (Protein Donor) |
O2A | OG1 | THR- 165 | 3 | 148.12 | H-Bond (Protein Donor) |
C4D | CB | THR- 165 | 3.87 | 0 | Hydrophobic |
N6A | O | VAL- 204 | 2.79 | 154.72 | H-Bond (Ligand Donor) |
N1A | N | VAL- 204 | 3.14 | 149.68 | H-Bond (Protein Donor) |
O1N | N | ALA- 417 | 2.81 | 137.94 | H-Bond (Protein Donor) |
C5D | CB | ALA- 417 | 3.98 | 0 | Hydrophobic |
C5N | CB | ALA- 417 | 4.39 | 0 | Hydrophobic |
C5N | CD2 | LEU- 422 | 4.15 | 0 | Hydrophobic |
C4N | CB | LEU- 422 | 3.88 | 0 | Hydrophobic |
C3D | CB | THR- 424 | 4.39 | 0 | Hydrophobic |
O3D | OG1 | THR- 424 | 2.72 | 172.48 | H-Bond (Ligand Donor) |
O2D | OG1 | THR- 424 | 3.32 | 169.03 | H-Bond (Ligand Donor) |
C3D | CB | ALA- 427 | 4.5 | 0 | Hydrophobic |
O1N | O | HOH- 970 | 2.69 | 179.94 | H-Bond (Protein Donor) |
O2N | O | HOH- 978 | 2.62 | 179.96 | H-Bond (Protein Donor) |