1JDF
Glucarate Dehydratase from E.coli N341D mutant
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0008872 | molecular_function | glucarate dehydratase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0019394 | biological_process | glucarate catabolic process |
| A | 0042838 | biological_process | D-glucarate catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0008872 | molecular_function | glucarate dehydratase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0019394 | biological_process | glucarate catabolic process |
| B | 0042838 | biological_process | D-glucarate catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0008872 | molecular_function | glucarate dehydratase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0019394 | biological_process | glucarate catabolic process |
| C | 0042838 | biological_process | D-glucarate catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0008872 | molecular_function | glucarate dehydratase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0019394 | biological_process | glucarate catabolic process |
| D | 0042838 | biological_process | D-glucarate catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 4500 |
| Chain | Residue |
| A | ASP235 |
| A | GLU260 |
| A | ASN289 |
| A | GLR2510 |
| A | HOH4655 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 4501 |
| Chain | Residue |
| B | HOH4638 |
| B | ASP235 |
| B | GLU260 |
| B | ASN289 |
| B | GLR2511 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 4502 |
| Chain | Residue |
| C | ASP235 |
| C | GLU260 |
| C | ASN289 |
| C | GLR2512 |
| C | HOH4698 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 4503 |
| Chain | Residue |
| D | ASP235 |
| D | GLU260 |
| D | ASN289 |
| D | GLR2513 |
| D | HOH4679 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GLR A 2510 |
| Chain | Residue |
| A | ASN27 |
| A | HIS32 |
| A | THR103 |
| A | PHE104 |
| A | TYR150 |
| A | PHE152 |
| A | LYS205 |
| A | LYS207 |
| A | ASP235 |
| A | ASN237 |
| A | GLU260 |
| A | ASN289 |
| A | HIS339 |
| A | SER340 |
| A | ASP341 |
| A | HIS368 |
| A | ARG422 |
| A | MG4500 |
| A | HOH4625 |
| A | HOH4654 |
| A | HOH4753 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE GLR B 2511 |
| Chain | Residue |
| B | ASN27 |
| B | HIS32 |
| B | THR103 |
| B | TYR150 |
| B | PHE152 |
| B | LYS205 |
| B | LYS207 |
| B | ASP235 |
| B | ASN237 |
| B | GLU260 |
| B | ASN289 |
| B | HIS339 |
| B | SER340 |
| B | ASP341 |
| B | HIS368 |
| B | ARG422 |
| B | MG4501 |
| B | HOH4562 |
| B | HOH4630 |
| site_id | AC7 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE GLR C 2512 |
| Chain | Residue |
| C | ASN27 |
| C | HIS32 |
| C | THR103 |
| C | TYR150 |
| C | PHE152 |
| C | LYS205 |
| C | LYS207 |
| C | ASP235 |
| C | ASN237 |
| C | GLU260 |
| C | ASN289 |
| C | HIS339 |
| C | SER340 |
| C | ASP341 |
| C | HIS368 |
| C | ARG422 |
| C | MG4502 |
| C | HOH4599 |
| C | HOH4650 |
| C | HOH4697 |
| site_id | AC8 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GLR D 2513 |
| Chain | Residue |
| D | HOH4647 |
| D | HOH4678 |
| D | ASN27 |
| D | HIS32 |
| D | THR103 |
| D | PHE104 |
| D | TYR150 |
| D | PHE152 |
| D | LYS205 |
| D | LYS207 |
| D | ASP235 |
| D | ASN237 |
| D | GLU260 |
| D | ASN289 |
| D | HIS339 |
| D | SER340 |
| D | ASP341 |
| D | HIS368 |
| D | ARG422 |
| D | MG4503 |
| D | HOH4638 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPA C 3601 |
| Chain | Residue |
| A | LEU302 |
| A | PHE332 |
| C | GLY299 |
| C | LEU302 |
| C | SER303 |
| C | HOH4699 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IPA D 3602 |
| Chain | Residue |
| B | LEU302 |
| B | PHE332 |
| B | HOH4603 |
| B | HOH4725 |
| D | GLY299 |
| D | LEU302 |
| D | SER303 |
| D | HOH4524 |
| D | HOH4810 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE IPA A 3603 |
| Chain | Residue |
| A | GLY299 |
| A | LEU302 |
| A | SER303 |
| C | LEU302 |
| C | PHE332 |
| C | HOH4699 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE IPA B 3604 |
| Chain | Residue |
| B | GLY299 |
| B | SER303 |
| B | HOH4603 |
| B | HOH4629 |
| D | LEU302 |
| D | PHE332 |
| D | HOH4518 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IPA A 3605 |
| Chain | Residue |
| A | ARG88 |
| A | ASP95 |
| A | ILE110 |
| A | HOH4713 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE IPA B 3606 |
| Chain | Residue |
| B | ARG88 |
| B | ASP95 |
| B | THR109 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IPA C 3607 |
| Chain | Residue |
| C | ARG88 |
| C | ALA92 |
| C | ASP95 |
| C | THR109 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE IPA D 3608 |
| Chain | Residue |
| D | ARG88 |
| D | ALA92 |
| D | ASP95 |
| D | HOH4623 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 44 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11513584","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| A | LYS207 | |
| A | ASP313 | |
| A | HIS339 | |
| A | ASP366 | |
| A | LYS205 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| B | LYS207 | |
| B | ASP313 | |
| B | HIS339 | |
| B | ASP366 | |
| B | LYS205 |
| site_id | CSA3 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| C | LYS207 | |
| C | ASP313 | |
| C | HIS339 | |
| C | ASP366 | |
| C | LYS205 |
| site_id | CSA4 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| D | LYS207 | |
| D | ASP313 | |
| D | HIS339 | |
| D | ASP366 | |
| D | LYS205 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| A | LYS207 | |
| A | ASP366 | |
| A | LYS205 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| B | LYS207 | |
| B | ASP366 | |
| B | LYS205 |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| C | LYS207 | |
| C | ASP366 | |
| C | LYS205 |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ec9 |
| Chain | Residue | Details |
| D | LYS207 | |
| D | ASP366 | |
| D | LYS205 |
| site_id | MCSA1 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| A | LYS205 | electrostatic stabiliser |
| A | LYS207 | electrostatic stabiliser |
| A | ASP235 | metal ligand |
| A | ASN237 | activator, electrostatic stabiliser |
| A | GLU260 | metal ligand |
| A | ASN289 | metal ligand |
| A | ASP313 | electrostatic stabiliser, modifies pKa |
| A | HIS339 | proton acceptor, proton donor |
| A | ASP341 | activator |
| site_id | MCSA2 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| B | LYS205 | electrostatic stabiliser |
| B | LYS207 | electrostatic stabiliser |
| B | ASP235 | metal ligand |
| B | ASN237 | activator, electrostatic stabiliser |
| B | GLU260 | metal ligand |
| B | ASN289 | metal ligand |
| B | ASP313 | electrostatic stabiliser, modifies pKa |
| B | HIS339 | proton acceptor, proton donor |
| B | ASP341 | activator |
| site_id | MCSA3 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| C | LYS205 | electrostatic stabiliser |
| C | LYS207 | electrostatic stabiliser |
| C | ASP235 | metal ligand |
| C | ASN237 | activator, electrostatic stabiliser |
| C | GLU260 | metal ligand |
| C | ASN289 | metal ligand |
| C | ASP313 | electrostatic stabiliser, modifies pKa |
| C | HIS339 | proton acceptor, proton donor |
| C | ASP341 | activator |
| site_id | MCSA4 |
| Number of Residues | 9 |
| Details | M-CSA 451 |
| Chain | Residue | Details |
| D | LYS205 | electrostatic stabiliser |
| D | LYS207 | electrostatic stabiliser |
| D | ASP235 | metal ligand |
| D | ASN237 | activator, electrostatic stabiliser |
| D | GLU260 | metal ligand |
| D | ASN289 | metal ligand |
| D | ASP313 | electrostatic stabiliser, modifies pKa |
| D | HIS339 | proton acceptor, proton donor |
| D | ASP341 | activator |
