1.800 Å
X-ray
2007-09-13
Name: | Beta-lactamase |
---|---|
ID: | AMPC_ECOLI |
AC: | P00811 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | 3.5.2.6 |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 100 % |
B-Factor: | 17.166 |
---|---|
Number of residues: | 30 |
Including | |
Standard Amino Acids: | 28 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.634 | 621.000 |
% Hydrophobic | % Polar |
---|---|
32.61 | 67.39 |
According to VolSite |
HET Code: | 23C |
---|---|
Formula: | C22H13NO6 |
Molecular weight: | 387.342 g/mol |
DrugBank ID: | DB06922 |
Buried Surface Area: | 47.5 % |
Polar Surface area: | 117.64 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 6 |
H-Bond Donors: | 0 |
Rings: | 4 |
Aromatic rings: | 3 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 5 |
X | Y | Z |
---|---|---|
22.6642 | 6.68955 | 14.2443 |
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 |
O | N | SER- 64 | 3.36 | 140.52 | H-Bond (Protein Donor) |
CAI | CG | LEU- 119 | 3.64 | 0 | Hydrophobic |
CAX | CD2 | LEU- 119 | 3.54 | 0 | Hydrophobic |
CD1 | CD1 | LEU- 119 | 3.82 | 0 | Hydrophobic |
CAI | CG | GLN- 120 | 3.39 | 0 | Hydrophobic |
CB | CE1 | TYR- 150 | 4.43 | 0 | Hydrophobic |
OAC | ND2 | ASN- 152 | 3.21 | 164.37 | H-Bond (Protein Donor) |
CAK | CG2 | VAL- 211 | 4.12 | 0 | Hydrophobic |
CAO | CG | TYR- 221 | 3.43 | 0 | Hydrophobic |
CAN | CD1 | LEU- 293 | 3.85 | 0 | Hydrophobic |
O | N | ALA- 318 | 2.9 | 154.93 | H-Bond (Protein Donor) |
CAP | CB | THR- 319 | 4.2 | 0 | Hydrophobic |
OAE | N | GLY- 320 | 2.81 | 149.16 | H-Bond (Protein Donor) |