3PWG
Crystal structure of the mutant S29G.P34A of D-Glucarate dehydratase from Escherichia coli complexed with product 5-keto-4-deoxy-D-Glucarate
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 447 |
Chain | Residue |
A | ASP235 |
A | GLU260 |
A | ASN289 |
A | GLR448 |
A | HOH502 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 447 |
Chain | Residue |
B | HOH514 |
B | ASP235 |
B | GLU260 |
B | ASN289 |
B | GLR448 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 447 |
Chain | Residue |
C | ASP235 |
C | ASN237 |
C | GLU260 |
C | ASN289 |
C | GLR448 |
C | HOH474 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 447 |
Chain | Residue |
D | ASP235 |
D | ASN237 |
D | GLU260 |
D | ASN289 |
D | GLR448 |
D | HOH463 |
site_id | AC5 |
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 | HOH488 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE GLR B 448 |
Chain | Residue |
B | ASN27 |
B | HIS32 |
B | THR103 |
B | PHE104 |
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 | HOH451 |
site_id | AC7 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE GLR C 448 |
Chain | Residue |
C | ASN27 |
C | HIS32 |
C | TYR150 |
C | PHE152 |
C | LYS205 |
C | LYS207 |
C | ASP235 |
C | ASN237 |
C | GLU260 |
C | ASN289 |
C | SER340 |
C | ASN341 |
C | HIS368 |
C | ARG422 |
C | MG447 |
site_id | AC8 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE GLR D 448 |
Chain | Residue |
D | ASN27 |
D | HIS32 |
D | TYR150 |
D | PHE152 |
D | LYS205 |
D | LYS207 |
D | ASP235 |
D | ASN237 |
D | GLU260 |
D | ASN289 |
D | SER340 |
D | HIS368 |
D | ARG422 |
D | MG447 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL A 449 |
Chain | Residue |
A | GLY299 |
A | SER303 |
A | HOH481 |
A | HOH485 |
B | ARG280 |
C | LEU302 |
C | PHE332 |
site_id | BC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL B 449 |
Chain | Residue |
D | PHE332 |
A | ARG280 |
B | GLY299 |
B | SER303 |
B | HOH483 |
D | LEU302 |
D | GLN305 |
site_id | BC2 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE GOL D 449 |
Chain | Residue |
B | LEU302 |
B | PHE332 |
B | HOH483 |
C | ARG280 |
D | GLY299 |
D | SER303 |
D | HOH456 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:11513584 |
Chain | Residue | Details |
A | LYS207 | |
A | HIS339 | |
B | LYS207 | |
B | HIS339 | |
C | LYS207 | |
C | HIS339 | |
D | LYS207 | |
D | HIS339 |
site_id | SWS_FT_FI2 |
Number of Residues | 32 |
Details | BINDING: |
Chain | Residue | Details |
A | HIS32 | |
B | THR103 | |
B | TYR150 | |
B | LYS205 | |
B | ASN289 | |
B | HIS339 | |
B | HIS368 | |
B | ARG422 | |
C | HIS32 | |
C | THR103 | |
C | TYR150 | |
A | THR103 | |
C | LYS205 | |
C | ASN289 | |
C | HIS339 | |
C | HIS368 | |
C | ARG422 | |
D | HIS32 | |
D | THR103 | |
D | TYR150 | |
D | LYS205 | |
D | ASN289 | |
A | TYR150 | |
D | HIS339 | |
D | HIS368 | |
D | ARG422 | |
A | LYS205 | |
A | ASN289 | |
A | HIS339 | |
A | HIS368 | |
A | ARG422 | |
B | HIS32 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:11513584 |
Chain | Residue | Details |
A | ASP235 | |
A | GLU266 | |
B | ASP235 | |
B | GLU266 | |
C | ASP235 | |
C | GLU266 | |
D | ASP235 | |
D | 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 |
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 | ASN341 | 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 | ASN341 | activator |