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 | 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 | 0016310 | biological_process | phosphorylation |
A | 0046872 | molecular_function | metal ion 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 | 0016310 | biological_process | phosphorylation |
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 | ACT_SITE: ACT_SITE => ECO:0000305|PubMed:21963988, ECO:0007744|PDB:3MBI |
Chain | Residue | Details |
A | LYS184 | |
B | LYS184 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3LPN, ECO:0007744|PDB:3LRT, ECO:0007744|PDB:3MBI, ECO:0007744|PDB:3NAG |
Chain | Residue | Details |
A | ASP34 | |
A | SER214 | |
B | ASP34 | |
B | SER214 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3LPN, ECO:0007744|PDB:3LRT, ECO:0007744|PDB:3MBI, ECO:0007744|PDB:3NAG |
Chain | Residue | Details |
A | ARG91 | |
B | ARG91 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:28031352 |
Chain | Residue | Details |
A | HIS124 | |
B | HIS124 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583 |
Chain | Residue | Details |
A | ASP161 | |
B | ASP161 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:21963988, ECO:0007744|PDB:3MBI |
Chain | Residue | Details |
A | ARG186 | |
A | ASP210 | |
B | ARG186 | |
B | ASP210 |