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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 447 |
Chain | Residue |
A | ASP235 |
A | ASN237 |
A | GLU260 |
A | ASP261 |
A | ASN289 |
A | GLR448 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 447 |
Chain | Residue |
B | ASP261 |
B | ASN289 |
B | GLR448 |
B | ASP235 |
B | ASN237 |
B | GLU260 |
site_id | AC3 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE GLR A 448 |
Chain | Residue |
A | ASN27 |
A | HIS32 |
A | THR103 |
A | TYR150 |
A | LYS205 |
A | LYS207 |
A | ASP235 |
A | ASN237 |
A | GLU260 |
A | ASN289 |
A | HIS339 |
A | SER340 |
A | ASN341 |
A | HIS368 |
A | ARG422 |
A | MG447 |
A | HOH492 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE GLR B 448 |
Chain | Residue |
B | ASN27 |
B | HIS32 |
B | THR103 |
B | TYR150 |
B | LYS205 |
B | LYS207 |
B | ASP235 |
B | ASN237 |
B | GLU260 |
B | ASN289 |
B | HIS339 |
B | SER340 |
B | ASN341 |
B | HIS368 |
B | ARG422 |
B | MG447 |
B | HOH455 |
B | HOH464 |
site_id | AC5 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL B 449 |
Chain | Residue |
A | ARG280 |
B | GLY299 |
B | LEU302 |
B | SER303 |
B | PHE332 |
B | HOH523 |
B | HOH523 |
B | HOH535 |
B | HOH544 |
site_id | AC6 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE GOL A 449 |
Chain | Residue |
A | GLY299 |
A | LEU302 |
A | SER303 |
A | GLN305 |
A | PHE332 |
A | HOH467 |
A | HOH485 |
A | HOH485 |
B | ARG280 |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LYS207 | |
A | HIS339 | |
B | LYS207 | |
B | HIS339 | |
site_id | SWS_FT_FI2 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS32 | |
B | THR103 | |
B | TYR150 | |
B | LYS205 | |
B | ASN289 | |
B | HIS339 | |
B | HIS368 | |
B | ARG422 | |
A | THR103 | |
A | TYR150 | |
A | LYS205 | |
A | ASN289 | |
A | HIS339 | |
A | HIS368 | |
A | ARG422 | |
B | HIS32 | |
Chain | Residue | Details |
A | ASP235 | |
A | GLU266 | |
B | ASP235 | |
B | GLU266 | |
Catalytic Information from CSA
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 | ASN341 | 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 | ASN341 | activator |