1IBS
PHOSPHORIBOSYLDIPHOSPHATE SYNTHETASE IN COMPLEX WITH CADMIUM IONS
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 | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| 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 | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase 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 SO4 B 1001 |
| Chain | Residue |
| B | ASP227 |
| B | THR228 |
| B | ALA229 |
| B | GLY230 |
| B | THR231 |
| B | HOH1015 |
| B | HOH1029 |
| B | HOH1035 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1002 |
| Chain | Residue |
| A | THR228 |
| A | ALA229 |
| A | GLY230 |
| A | THR231 |
| A | ASP227 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1003 |
| Chain | Residue |
| A | ARG109 |
| B | SER52 |
| B | ARG54 |
| B | SER310 |
| B | VAL311 |
| B | SER312 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1004 |
| Chain | Residue |
| A | SER52 |
| A | ARG54 |
| A | SER310 |
| A | VAL311 |
| A | SER312 |
| A | HOH1016 |
| A | HOH1018 |
| B | ARG109 |
| site_id | AC5 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CD A 1005 |
| Chain | Residue |
| A | HIS135 |
| A | ABM1009 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CD A 1006 |
| Chain | Residue |
| A | ASP174 |
| A | ASP223 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CD B 1007 |
| Chain | Residue |
| B | HIS135 |
| B | ABM1010 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CD B 1008 |
| Chain | Residue |
| B | ASP174 |
| B | ASP223 |
| B | HOH1033 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ABM A 1009 |
| Chain | Residue |
| A | ARG101 |
| A | GLN102 |
| A | ARG104 |
| A | HIS135 |
| A | CD1005 |
| A | HOH1030 |
| B | PHE40 |
| B | ASP42 |
| B | GLU44 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ABM B 1010 |
| Chain | Residue |
| A | PHE40 |
| A | ASP42 |
| A | GLU44 |
| A | GLN46 |
| B | ARG101 |
| B | GLN102 |
| B | ARG104 |
| B | HIS135 |
| B | CD1007 |
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 | Active site: {"evidences":[{"source":"PubMed","id":"28031352","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"16008562","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10742175","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11790837","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10742175","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1DKU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IBS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10742175","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1DKU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28031352","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"11790837","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1IBS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q97CA5","evidenceCode":"ECO:0000250"},{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"10742175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11790837","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DKR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1IBS","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| A | ASP224 | |
| A | ASP223 | |
| A | ASP227 | |
| A | CYS250 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1a95 |
| Chain | Residue | Details |
| B | ASP224 | |
| B | ASP223 | |
| B | ASP227 | |
| B | CYS250 |
