3TW9
Crystal structure of gluconate dehydratase (TARGET EFI-501679) from Salmonella enterica subsp. enterica serovar Enteritidis str. P125109
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0009063 | biological_process | amino acid catabolic process |
A | 0016052 | biological_process | carbohydrate catabolic process |
A | 0016829 | molecular_function | lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0047929 | molecular_function | gluconate dehydratase activity |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0009063 | biological_process | amino acid catabolic process |
B | 0016052 | biological_process | carbohydrate catabolic process |
B | 0016829 | molecular_function | lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0047929 | molecular_function | gluconate dehydratase activity |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0009063 | biological_process | amino acid catabolic process |
C | 0016052 | biological_process | carbohydrate catabolic process |
C | 0016829 | molecular_function | lyase activity |
C | 0046872 | molecular_function | metal ion binding |
C | 0047929 | molecular_function | gluconate dehydratase activity |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0009063 | biological_process | amino acid catabolic process |
D | 0016052 | biological_process | carbohydrate catabolic process |
D | 0016829 | molecular_function | lyase activity |
D | 0046872 | molecular_function | metal ion binding |
D | 0047929 | molecular_function | gluconate dehydratase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL A 420 |
Chain | Residue |
A | GLN45 |
B | TRP83 |
A | HIS227 |
A | GLU277 |
A | HIS327 |
A | PRO329 |
A | ASP331 |
A | HOH537 |
A | HOH964 |
B | TYR82 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 421 |
Chain | Residue |
A | GLY86 |
A | PRO87 |
A | ILE88 |
B | GLY86 |
B | ILE88 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 422 |
Chain | Residue |
A | GLN156 |
A | MET157 |
A | TYR201 |
A | ARG229 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL A 423 |
Chain | Residue |
A | ASP252 |
A | GLY276 |
A | GLU277 |
A | LEU278 |
A | HOH466 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 420 |
Chain | Residue |
A | TYR82 |
A | TRP83 |
B | GLN45 |
B | HIS227 |
B | GLU277 |
B | HIS327 |
B | PRO329 |
B | ASP331 |
B | HOH587 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 421 |
Chain | Residue |
B | GLN156 |
B | MET157 |
B | TYR201 |
B | ARG229 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL B 422 |
Chain | Residue |
B | ASP252 |
B | GLY276 |
B | GLU277 |
B | LEU278 |
B | HOH471 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL C 420 |
Chain | Residue |
C | GLN45 |
C | TYR82 |
C | TRP83 |
C | HIS227 |
C | GLU277 |
C | HIS327 |
C | PRO329 |
C | ASP331 |
C | HOH503 |
site_id | AC9 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL C 421 |
Chain | Residue |
C | GLY86 |
C | GLY86 |
C | PRO87 |
C | PRO87 |
C | ILE88 |
C | ILE88 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE CL C 422 |
Chain | Residue |
C | GLN156 |
C | MET157 |
C | ARG229 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL C 423 |
Chain | Residue |
C | HIS129 |
C | THR130 |
C | ASP131 |
C | ARG154 |
C | CL424 |
site_id | BC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE CL C 424 |
Chain | Residue |
C | THR130 |
C | VAL138 |
C | GLN156 |
C | CL423 |
C | HOH658 |
site_id | BC4 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE GOL D 420 |
Chain | Residue |
D | GLN45 |
D | TYR82 |
D | TRP83 |
D | HIS227 |
D | GLU277 |
D | HIS327 |
D | PRO329 |
D | ASP331 |
D | HOH680 |
D | HOH820 |
site_id | BC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL D 421 |
Chain | Residue |
D | GLN156 |
D | MET157 |
D | TYR201 |
D | ARG229 |
site_id | BC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE CL D 422 |
Chain | Residue |
D | GLY86 |
D | GLY86 |
D | PRO87 |
D | PRO87 |
D | ILE88 |
D | ILE88 |
Functional Information from PROSITE/UniProt
site_id | PS00908 |
Number of Residues | 26 |
Details | MR_MLE_1 Mandelate racemase / muconate lactonizing enzyme family signature 1. AlSGVDmALwDIkGKlagmPVydLLG |
Chain | Residue | Details |
A | ALA92-GLY117 |
site_id | PS00909 |
Number of Residues | 32 |
Details | MR_MLE_2 Mandelate racemase / muconate lactonizing enzyme family signature 2. FihDvHervtpvtAinlaktLeqyqlfyLEDP |
Chain | Residue | Details |
A | PHE222-PRO253 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton donor/acceptor => ECO:0000250 |
Chain | Residue | Details |
A | TYR160 | |
A | HIS227 | |
B | TYR160 | |
B | HIS227 | |
C | TYR160 | |
C | HIS227 | |
D | TYR160 | |
D | HIS227 |
site_id | SWS_FT_FI2 |
Number of Residues | 24 |
Details | BINDING: |
Chain | Residue | Details |
C | GLN45 | |
C | GLU277 | |
C | ARG298 | |
C | HIS327 | |
C | ASP331 | |
C | GLU354 | |
D | GLN45 | |
D | GLU277 | |
D | ARG298 | |
D | HIS327 | |
D | ASP331 | |
D | GLU354 | |
A | GLN45 | |
A | GLU277 | |
A | ARG298 | |
A | HIS327 | |
A | ASP331 | |
A | GLU354 | |
B | GLN45 | |
B | GLU277 | |
B | ARG298 | |
B | HIS327 | |
B | ASP331 | |
B | GLU354 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250 |
Chain | Residue | Details |
B | HIS129 | |
C | HIS129 | |
D | HIS129 | |
A | HIS129 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:24697546 |
Chain | Residue | Details |
C | ASP225 | |
C | GLU251 | |
D | ASP225 | |
D | GLU251 | |
A | ASP225 | |
A | GLU251 | |
B | ASP225 | |
B | GLU251 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity => ECO:0000250 |
Chain | Residue | Details |
A | PRO329 | |
B | PRO329 | |
C | PRO329 | |
D | PRO329 |