1XBZ
Crystal structure of 3-keto-L-gulonate 6-phosphate decarboxylase E112D/R139V/T169A mutant with bound L-xylulose 5-phosphate
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
A | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0019854 | biological_process | L-ascorbic acid catabolic process |
A | 0033982 | molecular_function | 3-dehydro-L-gulonate-6-phosphate decarboxylase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004590 | molecular_function | orotidine-5'-phosphate decarboxylase activity |
B | 0006207 | biological_process | 'de novo' pyrimidine nucleobase biosynthetic process |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0019854 | biological_process | L-ascorbic acid catabolic process |
B | 0033982 | molecular_function | 3-dehydro-L-gulonate-6-phosphate decarboxylase activity |
B | 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 601 |
Chain | Residue |
A | GLU33 |
A | ASP62 |
A | LX1501 |
A | HOH746 |
A | HOH755 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 602 |
Chain | Residue |
A | HOH755 |
A | GLU33 |
A | ASP62 |
A | LX1501 |
A | HOH746 |
site_id | AC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE LX1 A 501 |
Chain | Residue |
A | ALA9 |
A | ASP11 |
A | GLU33 |
A | ASP62 |
A | LYS64 |
A | HIS136 |
A | ALA169 |
A | GLY171 |
A | ILE189 |
A | GLY191 |
A | ARG192 |
A | MG601 |
A | MG602 |
A | HOH605 |
A | HOH612 |
A | HOH627 |
A | HOH714 |
A | HOH746 |
A | HOH755 |
B | ASP67 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE LX1 B 502 |
Chain | Residue |
A | ASP67 |
B | ALA9 |
B | ASP11 |
B | GLU33 |
B | ASP62 |
B | LYS64 |
B | HIS136 |
B | ALA169 |
B | GLY171 |
B | GLY191 |
B | ARG192 |
B | HOH503 |
B | HOH511 |
B | HOH519 |
B | HOH686 |
B | HOH705 |
B | HOH707 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | BINDING: |
Chain | Residue | Details |
B | ASP11 | |
B | GLU33 | |
B | ASP62 | |
B | ARG192 | |
A | ASP11 | |
A | GLU33 | |
A | ASP62 | |
A | ARG192 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | LYS64 | |
A | ASP67 | |
B | LYS64 | |
B | ASP67 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 9 |
Details | M-CSA 236 |
Chain | Residue | Details |
A | THR36 | ground state destabiliser |
A | ILE37 | ground state destabiliser |
A | LYS64 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
A | ASP67 | electrostatic stabiliser, hydrogen bond acceptor |
A | ALA68 | ground state destabiliser |
A | LEU72 | ground state destabiliser |
A | ASP112 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
A | HIS136 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | VAL139 | hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 9 |
Details | M-CSA 236 |
Chain | Residue | Details |
B | THR36 | ground state destabiliser |
B | ILE37 | ground state destabiliser |
B | LYS64 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
B | ASP67 | electrostatic stabiliser, hydrogen bond acceptor |
B | ALA68 | ground state destabiliser |
B | LEU72 | ground state destabiliser |
B | ASP112 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
B | HIS136 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | VAL139 | hydrogen bond donor, proton acceptor, proton donor |