1.950 Å
X-ray
2007-09-12
Name: | Citrate synthase |
---|---|
ID: | CISY_THEAC |
AC: | P21553 |
Organism: | Thermoplasma acidophilum |
Reign: | Archaea |
TaxID: | 273075 |
EC Number: | 2.3.3.16 |
Chain Name: | Percentage of Residues within binding site |
---|---|
C | 90 % |
D | 10 % |
B-Factor: | 19.433 |
---|---|
Number of residues: | 53 |
Including | |
Standard Amino Acids: | 50 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 3 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.140 | 624.375 |
% Hydrophobic | % Polar |
---|---|
42.70 | 57.30 |
According to VolSite |
HET Code: | SDX |
---|---|
Formula: | C28H41N7O22P3 |
Molecular weight: | 920.580 g/mol |
DrugBank ID: | - |
Buried Surface Area: | 60.23 % |
Polar Surface area: | 512.61 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 26 |
H-Bond Donors: | 7 |
Rings: | 3 |
Aromatic rings: | 2 |
Anionic atoms: | 6 |
Cationic atoms: | 1 |
Rule of Five Violation: | 3 |
Rotatable Bonds: | 26 |
X | Y | Z |
---|---|---|
7.08797 | 61.4547 | -18.3061 |
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 |
C40 | CB | PRO- 190 | 3.82 | 0 | Hydrophobic |
NP4 | O | LEU- 221 | 2.9 | 161.39 | H-Bond (Ligand Donor) |
CP6 | CD2 | LEU- 221 | 4.42 | 0 | Hydrophobic |
CQ4 | CB | LEU- 221 | 4.37 | 0 | Hydrophobic |
O2 | ND1 | HIS- 222 | 2.84 | 169.21 | H-Bond (Protein Donor) |
CP6 | CB | ALA- 225 | 4.27 | 0 | Hydrophobic |
OP9 | NH2 | ARG- 256 | 2.88 | 164.21 | H-Bond (Protein Donor) |
OA1 | NH1 | ARG- 256 | 2.81 | 136.72 | H-Bond (Protein Donor) |
OA1 | NH2 | ARG- 256 | 2.71 | 141.89 | H-Bond (Protein Donor) |
OA1 | CZ | ARG- 256 | 3.17 | 0 | Ionic (Protein Cationic) |
NA1 | N | LEU- 257 | 3.03 | 148.54 | H-Bond (Protein Donor) |
NA6 | O | LEU- 257 | 2.83 | 155.37 | H-Bond (Ligand Donor) |
CP6 | CE | MET- 258 | 3.74 | 0 | Hydrophobic |
OP5 | N | GLY- 259 | 2.79 | 145.06 | H-Bond (Protein Donor) |
NA6 | O | PHE- 260 | 2.92 | 133.25 | H-Bond (Ligand Donor) |
O20 | NE2 | HIS- 262 | 2.68 | 147.17 | H-Bond (Protein Donor) |
OA4 | CZ | ARG- 263 | 3.66 | 0 | Ionic (Protein Cationic) |
OA5 | CZ | ARG- 263 | 3.7 | 0 | Ionic (Protein Cationic) |
OA4 | NE | ARG- 263 | 2.71 | 158.94 | H-Bond (Protein Donor) |
OA5 | NH1 | ARG- 263 | 2.9 | 159.86 | H-Bond (Protein Donor) |
O31 | NH2 | ARG- 271 | 2.57 | 170.01 | H-Bond (Protein Donor) |
O20 | NH1 | ARG- 271 | 2.72 | 172.86 | H-Bond (Protein Donor) |
O31 | CZ | ARG- 271 | 3.51 | 0 | Ionic (Protein Cationic) |
CB1 | CD1 | ILE- 312 | 3.95 | 0 | Hydrophobic |
C1 | CB | ASN- 315 | 4.26 | 0 | Hydrophobic |
OP5 | ND2 | ASN- 315 | 2.98 | 163.54 | H-Bond (Protein Donor) |
C3 | CG2 | THR- 316 | 4.05 | 0 | Hydrophobic |
C3 | CZ | PHE- 340 | 3.84 | 0 | Hydrophobic |
O32 | NH1 | ARG- 344 | 2.72 | 173.48 | H-Bond (Protein Donor) |
O32 | NH2 | ARG- 344 | 3.45 | 128.7 | H-Bond (Protein Donor) |
O31 | NH2 | ARG- 344 | 2.67 | 165.22 | H-Bond (Protein Donor) |
O32 | CZ | ARG- 344 | 3.52 | 0 | Ionic (Protein Cationic) |
O31 | CZ | ARG- 344 | 3.53 | 0 | Ionic (Protein Cationic) |
OA2 | CZ | ARG- 361 | 3.63 | 0 | Ionic (Protein Cationic) |
OA2 | NE | ARG- 361 | 3 | 154.32 | H-Bond (Protein Donor) |
OA2 | NH2 | ARG- 361 | 3.41 | 133.13 | H-Bond (Protein Donor) |
CQ4 | CD2 | LEU- 362 | 4.08 | 0 | Hydrophobic |
O51 | CZ | ARG- 364 | 3.62 | 0 | Ionic (Protein Cationic) |
O52 | CZ | ARG- 364 | 3.59 | 0 | Ionic (Protein Cationic) |
O51 | NH2 | ARG- 364 | 2.76 | 173.22 | H-Bond (Protein Donor) |
O52 | NE | ARG- 364 | 2.79 | 178.45 | H-Bond (Protein Donor) |
O52 | NH2 | ARG- 364 | 3.49 | 130.93 | H-Bond (Protein Donor) |