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 |
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 |
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 |
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 |
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 | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00169 |
Chain | Residue | Details |
A | TYR26 | |
B | TYR26 | |
C | TYR26 | |
D | TYR26 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00169 |
Chain | Residue | Details |
A | HIS103 | |
B | HIS103 | |
C | HIS103 | |
D | HIS103 |
site_id | SWS_FT_FI3 |
Number of Residues | 20 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00169 |
Chain | Residue | Details |
A | ASN77 | |
B | ARG114 | |
C | ASN77 | |
C | HIS83 | |
C | ASP90 | |
C | LEU104 | |
C | ARG114 | |
D | ASN77 | |
D | HIS83 | |
D | ASP90 | |
D | LEU104 | |
A | HIS83 | |
D | ARG114 | |
A | ASP90 | |
A | LEU104 | |
A | ARG114 | |
B | ASN77 | |
B | HIS83 | |
B | ASP90 | |
B | LEU104 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_00169 |
Chain | Residue | Details |
A | ARG21 | |
B | ARG21 | |
C | ARG21 | |
D | ARG21 |