2.350 Å
X-ray
2004-07-13
Name: | Methionine aminotransferase |
---|---|
ID: | YBDL_ECOLI |
AC: | P77806 |
Organism: | Escherichia coli |
Reign: | Bacteria |
TaxID: | 83333 |
EC Number: | / |
Chain Name: | Percentage of Residues within binding site |
---|---|
A | 91 % |
B | 9 % |
B-Factor: | 23.571 |
---|---|
Number of residues: | 35 |
Including | |
Standard Amino Acids: | 33 |
Non Standard Amino Acids: | 0 |
Water Molecules: | 2 |
Cofactors: | |
Metals: |
Ligandability | Volume (Å3) |
---|---|
0.948 | 806.625 |
% Hydrophobic | % Polar |
---|---|
60.67 | 39.33 |
According to VolSite |
HET Code: | PLP |
---|---|
Formula: | C8H8NO6P |
Molecular weight: | 245.126 g/mol |
DrugBank ID: | DB00114 |
Buried Surface Area: | 77.47 % |
Polar Surface area: | 132.42 Å2 |
Number of | |
---|---|
H-Bond Acceptors: | 7 |
H-Bond Donors: | 1 |
Rings: | 1 |
Aromatic rings: | 1 |
Anionic atoms: | 2 |
Cationic atoms: | 0 |
Rule of Five Violation: | 0 |
Rotatable Bonds: | 4 |
X | Y | Z |
---|---|---|
13.0677 | 14.5541 | 18.0222 |
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 |
C4A | CZ | TYR- 63 | 4.25 | 0 | Hydrophobic |
O2P | OH | TYR- 63 | 2.67 | 164.36 | H-Bond (Protein Donor) |
C5A | CB | ALA- 100 | 4.2 | 0 | Hydrophobic |
O1P | N | ALA- 100 | 2.73 | 168.77 | H-Bond (Protein Donor) |
O3P | N | THR- 101 | 2.89 | 160.68 | H-Bond (Protein Donor) |
O3P | OG1 | THR- 101 | 2.73 | 153.99 | H-Bond (Protein Donor) |
C2A | CG | TYR- 125 | 3.87 | 0 | Hydrophobic |
C4A | CZ | TYR- 125 | 3.86 | 0 | Hydrophobic |
C5A | CZ | TYR- 125 | 4.13 | 0 | Hydrophobic |
DuAr | DuAr | TYR- 125 | 3.61 | 0 | Aromatic Face/Face |
C2A | CB | ASN- 174 | 3.92 | 0 | Hydrophobic |
O3 | ND2 | ASN- 174 | 2.76 | 154.54 | H-Bond (Protein Donor) |
N1 | OD1 | ASP- 202 | 3.45 | 127.45 | H-Bond (Ligand Donor) |
N1 | OD2 | ASP- 202 | 2.71 | 168.11 | H-Bond (Ligand Donor) |
C2A | CG2 | VAL- 204 | 3.86 | 0 | Hydrophobic |
C5 | CG1 | VAL- 204 | 4.45 | 0 | Hydrophobic |
C3 | CG2 | VAL- 204 | 3.96 | 0 | Hydrophobic |
C2A | CE2 | TYR- 205 | 3.95 | 0 | Hydrophobic |
O1P | OG | SER- 233 | 2.61 | 156.33 | H-Bond (Protein Donor) |
C4A | CD | LYS- 236 | 4.09 | 0 | Hydrophobic |
C4 | CE | LYS- 236 | 3.75 | 0 | Hydrophobic |
O2P | NZ | LYS- 244 | 3.34 | 128.29 | H-Bond (Protein Donor) |
O3P | NZ | LYS- 244 | 2.91 | 155.74 | H-Bond (Protein Donor) |
O2P | NZ | LYS- 244 | 3.34 | 0 | Ionic (Protein Cationic) |
O3P | NZ | LYS- 244 | 2.91 | 0 | Ionic (Protein Cationic) |