6SMF
THE CRYSTAL STRUCTURE OF TYPE II DEHYDROQUINASE FROM ZYMOMONAS MOBILIS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
A | 0008652 | biological_process | amino acid biosynthetic process |
A | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
A | 0009423 | biological_process | chorismate biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0019631 | biological_process | quinate catabolic process |
B | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
B | 0008652 | biological_process | amino acid biosynthetic process |
B | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
B | 0009423 | biological_process | chorismate biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0019631 | biological_process | quinate catabolic process |
C | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
C | 0008652 | biological_process | amino acid biosynthetic process |
C | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
C | 0009423 | biological_process | chorismate biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0019631 | biological_process | quinate catabolic process |
D | 0003855 | molecular_function | 3-dehydroquinate dehydratase activity |
D | 0008652 | biological_process | amino acid biosynthetic process |
D | 0009073 | biological_process | aromatic amino acid family biosynthetic process |
D | 0009423 | biological_process | chorismate biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0019631 | biological_process | quinate catabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | binding site for residue FLC A 201 |
Chain | Residue |
A | LEU15 |
A | ARG115 |
A | ASN78 |
A | ALA80 |
A | HIS84 |
A | HIS104 |
A | LEU105 |
A | SER106 |
A | PRO108 |
A | ARG111 |
site_id | AC2 |
Number of Residues | 6 |
Details | binding site for residue TRS A 202 |
Chain | Residue |
A | GLU57 |
A | THR85 |
B | GLU57 |
B | THR85 |
C | GLU57 |
C | THR85 |
site_id | AC3 |
Number of Residues | 12 |
Details | binding site for residue SO4 A 203 |
Chain | Residue |
A | HIS56 |
A | GLU57 |
A | GLY58 |
A | HOH302 |
B | HIS56 |
B | GLU57 |
B | GLY58 |
B | HOH305 |
C | HIS56 |
C | GLU57 |
C | GLY58 |
C | HOH301 |
site_id | AC4 |
Number of Residues | 11 |
Details | binding site for residue FLC B 201 |
Chain | Residue |
B | ASN78 |
B | ALA80 |
B | HIS84 |
B | HIS104 |
B | LEU105 |
B | SER106 |
B | PRO108 |
B | ARG111 |
B | ARG115 |
B | HOH308 |
B | HOH317 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue GOL B 202 |
Chain | Residue |
B | HIS116 |
C | LYS117 |
C | HOH302 |
site_id | AC6 |
Number of Residues | 8 |
Details | binding site for residue FLC C 201 |
Chain | Residue |
C | ASN78 |
C | ALA80 |
C | HIS84 |
C | HIS104 |
C | LEU105 |
C | SER106 |
C | ARG115 |
C | HOH310 |
site_id | AC7 |
Number of Residues | 9 |
Details | binding site for residue FLC D 201 |
Chain | Residue |
D | LEU15 |
D | ASN78 |
D | ALA80 |
D | HIS84 |
D | HIS104 |
D | LEU105 |
D | SER106 |
D | ARG111 |
D | ARG115 |
site_id | AC8 |
Number of Residues | 9 |
Details | binding site for residue TRS D 202 |
Chain | Residue |
D | GLU57 |
D | GLU57 |
D | GLU57 |
D | THR85 |
D | THR85 |
D | THR85 |
D | SER86 |
D | SER86 |
D | SER86 |
site_id | AC9 |
Number of Residues | 12 |
Details | binding site for residue SO4 D 203 |
Chain | Residue |
D | HIS56 |
D | HIS56 |
D | HIS56 |
D | GLU57 |
D | GLU57 |
D | GLU57 |
D | GLY58 |
D | GLY58 |
D | GLY58 |
D | HOH310 |
D | HOH310 |
D | HOH310 |
Functional Information from PROSITE/UniProt
site_id | PS01029 |
Number of Residues | 18 |
Details | DEHYDROQUINASE_II Dehydroquinase class II signature. LNGPNLnlLGlREptiYG |
Chain | Residue | Details |
A | LEU10-GLY27 |