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 |
