6VH5
Crystal structure of prephenate dehydratase from brucella melitensis biovar abortus 2308 in complex with phenylalanine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004106 | molecular_function | chorismate mutase activity |
A | 0004664 | molecular_function | prephenate dehydratase activity |
A | 0005737 | cellular_component | cytoplasm |
A | 0009094 | biological_process | L-phenylalanine biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016836 | molecular_function | hydro-lyase activity |
B | 0004106 | molecular_function | chorismate mutase activity |
B | 0004664 | molecular_function | prephenate dehydratase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0009094 | biological_process | L-phenylalanine biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016836 | molecular_function | hydro-lyase activity |
C | 0004106 | molecular_function | chorismate mutase activity |
C | 0004664 | molecular_function | prephenate dehydratase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0009094 | biological_process | L-phenylalanine biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0016836 | molecular_function | hydro-lyase activity |
D | 0004106 | molecular_function | chorismate mutase activity |
D | 0004664 | molecular_function | prephenate dehydratase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0009094 | biological_process | L-phenylalanine biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0016836 | molecular_function | hydro-lyase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 12 |
Details | binding site for residue PHE A 301 |
Chain | Residue |
A | ASN222 |
C | THR238 |
C | PHE240 |
C | EDO302 |
A | MET223 |
A | THR224 |
A | LYS225 |
C | ASN204 |
C | VAL205 |
C | ALA207 |
C | ALA208 |
C | LEU209 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 302 |
Chain | Residue |
A | ALA207 |
A | LEU209 |
A | TYR210 |
C | PHE216 |
C | VAL221 |
C | PHE301 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue PHE B 301 |
Chain | Residue |
B | ASN222 |
B | MET223 |
B | THR224 |
B | LYS225 |
D | ASN204 |
D | VAL205 |
D | ALA208 |
D | LEU209 |
D | SER228 |
D | THR238 |
D | PHE240 |
D | EDO302 |
site_id | AC4 |
Number of Residues | 7 |
Details | binding site for residue EDO B 302 |
Chain | Residue |
B | ALA207 |
B | ALA208 |
B | LEU209 |
B | TYR210 |
D | PHE216 |
D | VAL221 |
D | PHE301 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue EDO B 303 |
Chain | Residue |
B | LEU109 |
B | GLY123 |
site_id | AC6 |
Number of Residues | 12 |
Details | binding site for residue PHE C 301 |
Chain | Residue |
A | ASN204 |
A | VAL205 |
A | ALA207 |
A | ALA208 |
A | LEU209 |
A | THR238 |
A | PHE240 |
A | EDO302 |
C | ASN222 |
C | MET223 |
C | THR224 |
C | LYS225 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue EDO C 302 |
Chain | Residue |
A | PHE216 |
A | VAL221 |
A | PHE301 |
C | ALA207 |
C | ALA208 |
C | LEU209 |
C | TYR210 |
site_id | AC8 |
Number of Residues | 12 |
Details | binding site for residue PHE D 301 |
Chain | Residue |
B | ASN204 |
B | VAL205 |
B | ALA207 |
B | ALA208 |
B | LEU209 |
B | THR238 |
B | PHE240 |
B | EDO302 |
D | ASN222 |
D | MET223 |
D | THR224 |
D | LYS225 |
site_id | AC9 |
Number of Residues | 8 |
Details | binding site for residue EDO D 302 |
Chain | Residue |
B | PHE216 |
B | ALA217 |
B | VAL221 |
B | PHE301 |
D | ALA207 |
D | ALA208 |
D | LEU209 |
D | TYR210 |
site_id | AD1 |
Number of Residues | 5 |
Details | binding site for residue EDO D 303 |
Chain | Residue |
D | HIS66 |
D | TYR229 |
D | LEU231 |
D | GLN239 |
D | HOH416 |
Functional Information from PROSITE/UniProt
site_id | PS00857 |
Number of Residues | 23 |
Details | PREPHENATE_DEHYDR_1 Prephenate dehydratase signature 1. YgLdiLeenveDsennvTRFVvL |
Chain | Residue | Details |
A | TYR156-LEU178 |