6HSQ
The crystal structure of type II Dehydroquinase from Psychromonas ingrahamii 37 crystal form 1
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 | 6 |
| Details | binding site for residue SO4 A 201 |
| Chain | Residue |
| A | ASN77 |
| A | HIS103 |
| A | LEU104 |
| A | SER105 |
| A | GOL203 |
| A | HOH352 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 202 |
| Chain | Residue |
| A | HOH385 |
| A | ARG56 |
| A | HOH308 |
| A | HOH312 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | binding site for residue GOL A 203 |
| Chain | Residue |
| A | ASN77 |
| A | ALA79 |
| A | ALA80 |
| A | HIS83 |
| A | HIS103 |
| A | VAL107 |
| A | ARG110 |
| A | ARG114 |
| A | SO4201 |
| A | HOH344 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 201 |
| Chain | Residue |
| B | ASN77 |
| B | HIS103 |
| B | LEU104 |
| B | SER105 |
| B | GOL203 |
| B | HOH309 |
| B | HOH418 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 B 202 |
| Chain | Residue |
| B | ARG56 |
| B | HOH347 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 203 |
| Chain | Residue |
| B | ASN77 |
| B | ALA79 |
| B | ALA80 |
| B | HIS83 |
| B | HIS103 |
| B | ARG110 |
| B | ARG114 |
| B | SO4201 |
| B | HOH368 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 C 201 |
| Chain | Residue |
| C | ASN77 |
| C | HIS103 |
| C | LEU104 |
| C | SER105 |
| C | GOL203 |
| C | HOH328 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue SO4 C 202 |
| Chain | Residue |
| C | ARG56 |
| C | HOH353 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | binding site for residue GOL C 203 |
| Chain | Residue |
| C | ASN77 |
| C | ALA79 |
| C | ALA80 |
| C | HIS83 |
| C | HIS103 |
| C | ARG110 |
| C | ARG114 |
| C | SO4201 |
| C | HOH356 |
| site_id | AD1 |
| Number of Residues | 8 |
| Details | binding site for residue SO4 D 201 |
| Chain | Residue |
| D | ASN77 |
| D | HIS103 |
| D | LEU104 |
| D | SER105 |
| D | GOL203 |
| D | HOH363 |
| D | HOH421 |
| D | HOH432 |
| site_id | AD2 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 202 |
| Chain | Residue |
| D | ARG56 |
| D | HOH305 |
| D | HOH347 |
| D | HOH399 |
| site_id | AD3 |
| Number of Residues | 11 |
| Details | binding site for residue GOL D 203 |
| Chain | Residue |
| D | ASN77 |
| D | ALA79 |
| D | ALA80 |
| D | HIS83 |
| D | ASP90 |
| D | HIS103 |
| D | VAL107 |
| D | ARG110 |
| D | ARG114 |
| D | SO4201 |
| D | HOH404 |
Functional Information from PROSITE/UniProt
| site_id | PS01029 |
| Number of Residues | 18 |
| Details | DEHYDROQUINASE_II Dehydroquinase class II signature. LNGPNLnlLGqREpevYG |
| Chain | Residue | Details |
| A | LEU10-GLY27 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_00169","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
