1.990 Å
X-ray
2010-07-03
Name: | FAD-dependent pyridine nucleotide-disulphide oxidoreductase |
---|---|
ID: | A3QAV3_SHELP |
AC: | A3QAV3 |
Organism: | Shewanella loihica |
Reign: | Bacteria |
TaxID: | 323850 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 9 % |
B | 91 % |
B-Factor: | 29.966 |
---|---|
Number of residues: | 62 |
Including | |
Standard Amino Acids: | 57 |
Non Standard Amino Acids: | 1 |
Water Molecules: | 4 |
Cofactors: | COA |
Metals: |
Ligandability | Volume (Å3) |
---|---|
1.365 | 1265.625 |
% Hydrophobic | % Polar |
---|---|
47.73 | 52.27 |
According to VolSite |
HET Code: | FAD |
---|---|
Formula: | C27H31N9O15P2 |
Molecular weight: | 783.534 g/mol |
DrugBank ID: | DB03147 |
Buried Surface Area: | 75.69 % |
Polar Surface area: | 381.7 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 22 |
H-Bond Donors: | 7 |
Rings: | 6 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 13 |
X | Y | Z |
---|---|---|
9.29494 | -46.424 | 26.2643 |
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 |
C4B | CG2 | VAL- 10 | 3.98 | 0 | Hydrophobic |
C4' | CB | ALA- 11 | 3.85 | 0 | Hydrophobic |
O1P | N | GLY- 12 | 2.95 | 149.09 | H-Bond (Protein Donor) |
O3B | OE2 | GLU- 33 | 3 | 130.44 | H-Bond (Ligand Donor) |
O3B | OE1 | GLU- 33 | 2.77 | 161.67 | H-Bond (Ligand Donor) |
O2B | OE2 | GLU- 33 | 2.71 | 172.11 | H-Bond (Ligand Donor) |
N3A | N | ARG- 34 | 3.11 | 140.89 | H-Bond (Protein Donor) |
C2B | CD | ARG- 34 | 3.62 | 0 | Hydrophobic |
O2A | ND2 | ASN- 42 | 3.18 | 160.49 | H-Bond (Protein Donor) |
C8 | CB | ASN- 42 | 4.1 | 0 | Hydrophobic |
C6 | CB | CYS- 43 | 4.43 | 0 | Hydrophobic |
C9A | SG | CYS- 43 | 3.96 | 0 | Hydrophobic |
C7M | CG | PRO- 46 | 4.28 | 0 | Hydrophobic |
N6A | O | VAL- 81 | 2.93 | 158.86 | H-Bond (Ligand Donor) |
N1A | N | VAL- 81 | 3.04 | 160.3 | H-Bond (Protein Donor) |
O1P | OG | SER- 112 | 2.89 | 137.44 | H-Bond (Protein Donor) |
C7M | CD2 | LEU- 133 | 3.71 | 0 | Hydrophobic |
O1A | NH2 | ARG- 134 | 2.97 | 172.86 | H-Bond (Protein Donor) |
O1A | CZ | ARG- 134 | 3.82 | 0 | Ionic (Protein Cationic) |
C1' | CZ | PHE- 161 | 4.48 | 0 | Hydrophobic |
C7 | CG1 | ILE- 162 | 3.66 | 0 | Hydrophobic |
C8 | CD1 | ILE- 162 | 3.65 | 0 | Hydrophobic |
O3' | OD1 | ASP- 303 | 2.94 | 162.99 | H-Bond (Ligand Donor) |
O3' | OD2 | ASP- 303 | 3.47 | 135.19 | H-Bond (Ligand Donor) |
C5' | CB | ASP- 303 | 4.26 | 0 | Hydrophobic |
O2P | N | ASP- 303 | 2.73 | 165.73 | H-Bond (Protein Donor) |
N1 | N | ALA- 321 | 3.46 | 127.85 | H-Bond (Protein Donor) |
O2 | N | ALA- 321 | 2.89 | 176.09 | H-Bond (Protein Donor) |
C2' | CB | ALA- 321 | 3.93 | 0 | Hydrophobic |
C5' | CB | ALA- 324 | 4.18 | 0 | Hydrophobic |
N3 | O | TYR- 446 | 2.82 | 164.82 | H-Bond (Ligand Donor) |
O1P | O | HOH- 575 | 2.64 | 179.94 | H-Bond (Protein Donor) |
O2P | O | HOH- 585 | 2.92 | 179.96 | H-Bond (Protein Donor) |
C2' | C2P | COA- 901 | 4.19 | 0 | Hydrophobic |