2.600 Å
X-ray
2006-05-18
Name: | Ribulose-1,5 bisphosphate carboxylase/oxygenase large subunit N-methyltransferase, chloroplastic |
---|---|
ID: | RBCMT_PEA |
AC: | Q43088 |
Organism: | Pisum sativum |
Reign: | Eukaryota |
TaxID: | 3888 |
EC Number: | 2.1.1.127 |
Chain Name: | Percentage of Residues within binding site |
---|---|
C | 100 % |
B-Factor: | 56.027 |
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Number of residues: | 31 |
Including | |
Standard Amino Acids: | 30 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 1 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.534 | 594.000 |
% Hydrophobic | % Polar |
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40.91 | 59.09 |
According to VolSite |
HET Code: | SA8 |
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Formula: | C15H24N7O5 |
Molecular weight: | 382.395 g/mol |
DrugBank ID: | DB03458 |
Buried Surface Area: | 60.7 % |
Polar Surface area: | 191.52 Å2 |
Number of | |
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H-Bond Acceptors: | 9 |
H-Bond Donors: | 5 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 1 |
Cationic atoms: | 2 |
Rule of Five Violation: | 1 |
Rotatable Bonds: | 7 |
X | Y | Z |
---|---|---|
119.941 | 130.865 | 142.054 |
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 |
OXT | N | LEU- 82 | 2.94 | 160.07 | H-Bond (Protein Donor) |
O | NH2 | ARG- 222 | 2.94 | 147.32 | H-Bond (Protein Donor) |
N | OD1 | ASN- 242 | 3.43 | 155.85 | H-Bond (Ligand Donor) |
N7 | N | HIS- 243 | 2.83 | 153.95 | H-Bond (Protein Donor) |
N6 | O | HIS- 243 | 2.72 | 154.85 | H-Bond (Ligand Donor) |
C2' | CD2 | PHE- 302 | 3.96 | 0 | Hydrophobic |