1DKU
CRYSTAL STRUCTURES OF BACILLUS SUBTILIS PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE: MOLECULAR BASIS OF ALLOSTERIC INHIBITION AND ACTIVATION.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0002189 | cellular_component | ribose phosphate diphosphokinase complex |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0008152 | biological_process | metabolic process |
| A | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016310 | biological_process | phosphorylation |
| A | 0016740 | molecular_function | transferase activity |
| A | 0044249 | biological_process | cellular biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0002189 | cellular_component | ribose phosphate diphosphokinase complex |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0008152 | biological_process | metabolic process |
| B | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016310 | biological_process | phosphorylation |
| B | 0016740 | molecular_function | transferase activity |
| B | 0044249 | biological_process | cellular biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE AP2 B 1001 |
| Chain | Residue |
| A | LYS105 |
| B | VAL311 |
| B | SER312 |
| B | PHE315 |
| B | HOH1005 |
| B | HOH1006 |
| B | HOH1029 |
| A | SER108 |
| A | ARG109 |
| B | SER52 |
| B | ARG54 |
| B | GLN140 |
| B | ASP148 |
| B | HIS149 |
| B | SER310 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE AP2 A 1002 |
| Chain | Residue |
| A | SER52 |
| A | ARG54 |
| A | GLN140 |
| A | ASP148 |
| A | HIS149 |
| A | SER310 |
| A | VAL311 |
| A | SER312 |
| A | PHE315 |
| A | HOH1010 |
| B | LYS105 |
| B | ALA106 |
| B | ARG107 |
| B | SER108 |
| B | ARG109 |
| B | HOH1045 |
| site_id | AC3 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE ABM A 1003 |
| Chain | Residue |
| A | ARG101 |
| A | GLN102 |
| A | ALA106 |
| A | HIS135 |
| A | HOH1046 |
| A | HOH1096 |
| A | HOH1097 |
| A | HOH1098 |
| B | PHE40 |
| B | ASP42 |
| B | GLU44 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ABM B 1004 |
| Chain | Residue |
| A | PHE40 |
| A | ASP42 |
| A | GLU44 |
| B | ARG101 |
| B | GLN102 |
| B | ARG104 |
| B | ALA106 |
| B | GLU110 |
| B | HIS135 |
| B | HOH1088 |
Functional Information from PROSITE/UniProt
| site_id | PS00103 |
| Number of Residues | 13 |
| Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. AILIDDIIDTAgT |
| Chain | Residue | Details |
| A | ALA219-THR231 |
| site_id | PS00114 |
| Number of Residues | 16 |
| Details | PRPP_SYNTHASE Phosphoribosyl pyrophosphate synthase signature. DLHApQIQGFFdiPID |
| Chain | Residue | Details |
| A | ASP133-ASP148 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: ACT_SITE => ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:16008562 |
| Chain | Residue | Details |
| A | LYS197 | |
| B | LYS197 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:10742175 |
| Chain | Residue | Details |
| A | ASP42 | |
| B | ASP42 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:11790837, ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU, ECO:0007744|PDB:1IBS |
| Chain | Residue | Details |
| A | ARG101 | |
| B | ARG101 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000305|PubMed:10742175, ECO:0007744|PDB:1DKU |
| Chain | Residue | Details |
| A | LYS105 | |
| B | SER310 | |
| A | ARG109 | |
| A | GLN140 | |
| A | ASP148 | |
| A | SER310 | |
| B | LYS105 | |
| B | ARG109 | |
| B | GLN140 | |
| B | ASP148 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352, ECO:0000305|PubMed:11790837, ECO:0007744|PDB:1IBS |
| Chain | Residue | Details |
| A | HIS135 | |
| A | ASP174 | |
| B | HIS135 | |
| B | ASP174 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q97CA5, ECO:0000255|HAMAP-Rule:MF_00583 |
| Chain | Residue | Details |
| A | ARG199 | |
| A | ASP223 | |
| B | ARG199 | |
| B | ASP223 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:10742175, ECO:0000269|PubMed:11790837, ECO:0007744|PDB:1DKR, ECO:0007744|PDB:1IBS |
| Chain | Residue | Details |
| A | ASP227 | |
| B | ASP227 |
