1KV8
Crystal Structure of 3-Keto-L-Gulonate 6-Phosphate Decarboxylase
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 | 0016052 | biological_process | carbohydrate catabolic process |
| A | 0016829 | molecular_function | lyase activity |
| 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 | 0016052 | biological_process | carbohydrate catabolic process |
| B | 0016829 | molecular_function | lyase activity |
| 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 | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 B 501 |
| Chain | Residue |
| B | GLY171 |
| B | GLY191 |
| B | ARG192 |
| B | HOH503 |
| B | HOH515 |
| B | HOH517 |
| B | HOH520 |
| B | HOH571 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 502 |
| Chain | Residue |
| A | GLY191 |
| A | ARG192 |
| A | HOH505 |
| A | HOH511 |
| A | HOH519 |
| A | HOH540 |
| A | HOH552 |
| A | GLY171 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 503 |
| Chain | Residue |
| A | GLU33 |
| A | ASP62 |
| A | HOH520 |
| A | HOH535 |
| A | HOH634 |
| A | HOH645 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASP11 | |
| A | GLU33 | |
| A | ASP62 | |
| A | ARG192 | |
| B | ASP11 | |
| B | GLU33 | |
| B | ASP62 | |
| B | 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 | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| A | LYS64 | |
| A | ASP62 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dbt |
| Chain | Residue | Details |
| B | LYS64 | |
| B | ASP62 |
| 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 | GLU112 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
| A | HIS136 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | ARG139 | 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 | GLU112 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
| B | HIS136 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | ARG139 | hydrogen bond donor, proton acceptor, proton donor |
