1.800 Å
X-ray
2002-08-21
Name: | NAD(P)H-dependent D-xylose reductase |
---|---|
ID: | XYL1_CANTE |
AC: | O74237 |
Organism: | Candida tenuis |
Reign: | Eukaryota |
TaxID: | 45596 |
EC Number: | 1.1.1.307 |
Chain Name: | Percentage of Residues within binding site |
---|---|
C | 100 % |
B-Factor: | 23.672 |
---|---|
Number of residues: | 44 |
Including | |
Standard Amino Acids: | 43 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.548 | 907.875 |
% Hydrophobic | % Polar |
---|---|
43.87 | 56.13 |
According to VolSite |
HET Code: | NAD |
---|---|
Formula: | C21H26N7O14P2 |
Molecular weight: | 662.417 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 75.97 % |
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 |
---|---|---|
61.4204 | 120.432 | 69.2562 |
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 |
O2D | N | CYS- 23 | 3.44 | 128.63 | H-Bond (Protein Donor) |
O3D | N | TRP- 24 | 3.02 | 145.93 | H-Bond (Protein Donor) |
C3D | CB | TRP- 24 | 3.5 | 0 | Hydrophobic |
O2D | OD2 | ASP- 47 | 2.75 | 171.74 | H-Bond (Ligand Donor) |
C2D | CZ | TYR- 52 | 4.06 | 0 | Hydrophobic |
N7N | OG | SER- 169 | 2.87 | 135.85 | H-Bond (Ligand Donor) |
O7N | ND2 | ASN- 170 | 2.92 | 172.51 | H-Bond (Protein Donor) |
N7N | OE1 | GLN- 191 | 2.95 | 156.65 | H-Bond (Ligand Donor) |
C4D | CB | TYR- 217 | 4.49 | 0 | Hydrophobic |
C3N | CB | TYR- 217 | 4.2 | 0 | Hydrophobic |
C5N | CB | TYR- 217 | 4.38 | 0 | Hydrophobic |
DuAr | DuAr | TYR- 217 | 3.6 | 0 | Aromatic Face/Face |
O2N | OG | SER- 218 | 2.97 | 157.43 | H-Bond (Protein Donor) |
O5D | N | SER- 218 | 3.15 | 150.22 | H-Bond (Protein Donor) |
O1A | N | PHE- 220 | 3.1 | 157.4 | H-Bond (Protein Donor) |
C5B | CD1 | PHE- 220 | 4.34 | 0 | Hydrophobic |
C1B | CD1 | PHE- 220 | 4.49 | 0 | Hydrophobic |
C1B | CG | GLN- 223 | 4.09 | 0 | Hydrophobic |
C4B | CG | GLN- 223 | 3.55 | 0 | Hydrophobic |
C5B | CB | SER- 224 | 3.56 | 0 | Hydrophobic |
O2N | OG | SER- 224 | 2.63 | 141.78 | H-Bond (Protein Donor) |
O3B | OE2 | GLU- 227 | 3.37 | 135.92 | H-Bond (Ligand Donor) |
O2B | OE1 | GLU- 227 | 3.48 | 141.57 | H-Bond (Ligand Donor) |
O2B | OE2 | GLU- 227 | 2.7 | 159.18 | H-Bond (Ligand Donor) |
C5D | CG1 | ILE- 272 | 4.49 | 0 | Hydrophobic |
C4D | CD1 | ILE- 272 | 3.94 | 0 | Hydrophobic |
C2D | CD1 | ILE- 272 | 4.35 | 0 | Hydrophobic |
O2A | N | LYS- 274 | 2.99 | 159.05 | H-Bond (Protein Donor) |
C3B | CG | LYS- 274 | 3.74 | 0 | Hydrophobic |
C5D | CB | LYS- 274 | 4.45 | 0 | Hydrophobic |
DuAr | CZ | ARG- 280 | 3.66 | 152.87 | Pi/Cation |
N7A | ND2 | ASN- 284 | 2.99 | 168.45 | H-Bond (Protein Donor) |
N6A | OD1 | ASN- 284 | 2.96 | 156.73 | H-Bond (Ligand Donor) |