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 | 5 |
| Details | Active site: {"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24697546","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for activity and substrate specificity; Pro is observed in family members with low D-mannonate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
