1HO4
CRYSTAL STRUCTURE OF PYRIDOXINE 5'-PHOSPHATE SYNTHASE IN COMPLEX WITH PYRIDOXINE 5'-PHOSPHATE AND INORGANIC PHOSPHATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0008615 | biological_process | pyridoxine biosynthetic process |
A | 0016740 | molecular_function | transferase activity |
A | 0016769 | molecular_function | transferase activity, transferring nitrogenous groups |
A | 0033856 | molecular_function | pyridoxine 5'-phosphate synthase activity |
A | 0042802 | molecular_function | identical protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0008615 | biological_process | pyridoxine biosynthetic process |
B | 0016740 | molecular_function | transferase activity |
B | 0016769 | molecular_function | transferase activity, transferring nitrogenous groups |
B | 0033856 | molecular_function | pyridoxine 5'-phosphate synthase activity |
B | 0042802 | molecular_function | identical protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0008615 | biological_process | pyridoxine biosynthetic process |
C | 0016740 | molecular_function | transferase activity |
C | 0016769 | molecular_function | transferase activity, transferring nitrogenous groups |
C | 0033856 | molecular_function | pyridoxine 5'-phosphate synthase activity |
C | 0042802 | molecular_function | identical protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0008615 | biological_process | pyridoxine biosynthetic process |
D | 0016740 | molecular_function | transferase activity |
D | 0016769 | molecular_function | transferase activity, transferring nitrogenous groups |
D | 0033856 | molecular_function | pyridoxine 5'-phosphate synthase activity |
D | 0042802 | molecular_function | identical protein binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PO4 A 901 |
Chain | Residue |
A | ASP11 |
A | HOH993 |
A | HOH1093 |
A | HIS12 |
A | ARG20 |
A | HIS45 |
A | ARG47 |
A | HIS52 |
A | THR102 |
A | PXP802 |
A | HOH972 |
site_id | AC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 C 902 |
Chain | Residue |
B | ARG20 |
C | ASP11 |
C | HIS12 |
C | HIS45 |
C | ARG47 |
C | HIS52 |
C | THR102 |
C | PXP803 |
C | HOH1075 |
C | HOH1084 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PO4 B 903 |
Chain | Residue |
B | ASP11 |
B | HIS12 |
B | HIS45 |
B | ARG47 |
B | HIS52 |
B | THR102 |
B | PXP804 |
B | HOH956 |
B | HOH1070 |
C | ARG20 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PXP D 801 |
Chain | Residue |
D | ASN9 |
D | ARG20 |
D | GLU72 |
D | VAL94 |
D | PHE133 |
D | GLU153 |
D | HIS193 |
D | GLY194 |
D | ASN213 |
D | ILE214 |
D | GLY215 |
D | HIS216 |
D | HOH816 |
D | HOH850 |
D | HOH852 |
D | HOH969 |
D | HOH970 |
D | HOH992 |
site_id | AC5 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE PXP A 802 |
Chain | Residue |
A | ARG20 |
A | GLU72 |
A | VAL94 |
A | THR102 |
A | THR103 |
A | PHE133 |
A | GLU153 |
A | HIS193 |
A | GLY194 |
A | ASN213 |
A | ILE214 |
A | GLY215 |
A | HIS216 |
A | PO4901 |
A | HOH956 |
A | HOH968 |
A | HOH972 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PXP C 803 |
Chain | Residue |
B | ARG20 |
C | GLU72 |
C | VAL94 |
C | THR103 |
C | PHE133 |
C | GLU153 |
C | HIS193 |
C | GLY194 |
C | ASN213 |
C | ILE214 |
C | GLY215 |
C | HIS216 |
C | PO4902 |
C | HOH908 |
C | HOH915 |
C | HOH966 |
site_id | AC7 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PXP B 804 |
Chain | Residue |
B | GLU72 |
B | VAL94 |
B | THR103 |
B | GLU153 |
B | GLY192 |
B | HIS193 |
B | GLY194 |
B | ASN213 |
B | ILE214 |
B | GLY215 |
B | HIS216 |
B | PO4903 |
B | HOH909 |
B | HOH935 |
B | HOH956 |
C | ARG20 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | LEU46 | |
A | MET73 | |
B | LEU46 | |
B | MET73 | |
C | LEU46 | |
C | MET73 | |
D | LEU46 | |
D | MET73 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton donor |
Chain | Residue | Details |
A | GLY194 | |
B | GLY194 | |
C | GLY194 | |
D | GLY194 |
site_id | SWS_FT_FI3 |
Number of Residues | 32 |
Details | BINDING: |
Chain | Residue | Details |
B | ILE10 | |
B | HIS12 | |
B | GLY21 | |
B | GLU48 | |
B | ILE53 | |
B | THR103 | |
B | LEU195 | |
B | HIS216 | |
C | ILE10 | |
C | HIS12 | |
C | GLY21 | |
C | GLU48 | |
C | ILE53 | |
C | THR103 | |
C | LEU195 | |
C | HIS216 | |
D | ILE10 | |
D | HIS12 | |
D | GLY21 | |
D | GLU48 | |
D | ILE53 | |
D | THR103 | |
D | LEU195 | |
D | HIS216 | |
A | ILE10 | |
A | HIS12 | |
A | GLY21 | |
A | GLU48 | |
A | ILE53 | |
A | THR103 | |
A | LEU195 | |
A | HIS216 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | ILE154 | |
B | ILE154 | |
C | ILE154 | |
D | ILE154 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 9 |
Details | M-CSA 243 |
Chain | Residue | Details |
A | ILE10 | electrostatic stabiliser, hydrogen bond donor |
A | ILE13 | attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | LEU46 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | GLU48 | attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity |
A | HIS52 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity |
A | MET73 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
A | GLU104 | electrostatic stabiliser, hydrogen bond acceptor |
A | ILE154 | electrostatic stabiliser, hydrogen bond acceptor |
A | GLY194 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA2 |
Number of Residues | 9 |
Details | M-CSA 243 |
Chain | Residue | Details |
B | ILE10 | electrostatic stabiliser, hydrogen bond donor |
B | ILE13 | attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | LEU46 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | GLU48 | attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity |
B | HIS52 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity |
B | MET73 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
B | GLU104 | electrostatic stabiliser, hydrogen bond acceptor |
B | ILE154 | electrostatic stabiliser, hydrogen bond acceptor |
B | GLY194 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA3 |
Number of Residues | 9 |
Details | M-CSA 243 |
Chain | Residue | Details |
C | ILE10 | electrostatic stabiliser, hydrogen bond donor |
C | ILE13 | attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | LEU46 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | GLU48 | attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity |
C | HIS52 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity |
C | MET73 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
C | GLU104 | electrostatic stabiliser, hydrogen bond acceptor |
C | ILE154 | electrostatic stabiliser, hydrogen bond acceptor |
C | GLY194 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
site_id | MCSA4 |
Number of Residues | 9 |
Details | M-CSA 243 |
Chain | Residue | Details |
D | ILE10 | electrostatic stabiliser, hydrogen bond donor |
D | ILE13 | attractive charge-charge interaction, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | LEU46 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | GLU48 | attractive charge-charge interaction, electrostatic stabiliser, increase acidity, increase basicity |
D | HIS52 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, increase acidity, increase basicity |
D | MET73 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor, proton relay |
D | GLU104 | electrostatic stabiliser, hydrogen bond acceptor |
D | ILE154 | electrostatic stabiliser, hydrogen bond acceptor |
D | GLY194 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |