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 |
