3LRT
Crystal structure of the phosphoribosyl pyrophosphate (PRPP) synthetase from Thermoplasma volcanium in complex with ADP.
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 | 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 | 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 | 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 | 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 | 15 |
| Details | BINDING SITE FOR RESIDUE ADP B 300 |
| Chain | Residue |
| A | PHE32 |
| A | HOH477 |
| B | ARG91 |
| B | GLN92 |
| B | HIS93 |
| B | TYR96 |
| B | HOH342 |
| A | ASP34 |
| A | GLU36 |
| A | HOH298 |
| A | HOH320 |
| A | HOH338 |
| A | HOH370 |
| A | HOH399 |
| A | HOH465 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 287 |
| Chain | Residue |
| A | ARG91 |
| A | SER214 |
| A | THR215 |
| A | GLY216 |
| A | GLY217 |
| A | THR218 |
| A | HOH332 |
| A | HOH348 |
| A | HOH379 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 288 |
| Chain | Residue |
| A | ARG7 |
| A | SER58 |
| A | HOH310 |
| A | HOH419 |
| A | HOH450 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 289 |
| Chain | Residue |
| A | LYS11 |
| A | ARG15 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ADP A 300 |
| Chain | Residue |
| A | ARG91 |
| A | GLN92 |
| A | HIS93 |
| A | TYR96 |
| A | HIS124 |
| A | HOH386 |
| B | PHE32 |
| B | ASP34 |
| B | GLU36 |
| B | HOH322 |
| B | HOH325 |
| B | HOH326 |
| B | HOH346 |
| B | HOH349 |
| B | HOH368 |
| B | HOH496 |
| B | HOH499 |
| site_id | AC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 287 |
| Chain | Residue |
| B | ARG7 |
| B | SER58 |
| B | HOH339 |
| B | HOH425 |
Functional Information from PROSITE/UniProt
| site_id | PS00103 |
| Number of Residues | 13 |
| Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. LLIVDDIISTGgT |
| Chain | Residue | Details |
| A | LEU206-THR218 |
| site_id | PS00144 |
| Number of Residues | 9 |
| Details | ASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. IiSTGGTIA |
| Chain | Residue | Details |
| A | ILE212-ALA220 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"21963988","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"3MBI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21963988","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LPN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LRT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MBI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NAG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"21963988","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3LPN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LRT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3MBI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3NAG","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"28031352","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00583","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21963988","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3MBI","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
