3NAG
Crystal structure of the phosphoribosylpyrophosphate (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 | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| 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 | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 287 |
| Chain | Residue |
| A | SER214 |
| A | THR215 |
| A | GLY216 |
| A | GLY217 |
| A | THR218 |
| A | HOH395 |
| A | HOH436 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 288 |
| Chain | Residue |
| A | ALA60 |
| A | HOH294 |
| A | HOH336 |
| A | HOH379 |
| A | ARG7 |
| A | SER58 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE SO4 A 289 |
| Chain | Residue |
| A | LYS11 |
| A | ARG15 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE ADP B 300 |
| Chain | Residue |
| A | PHE32 |
| A | ASP34 |
| A | GLU36 |
| A | HOH295 |
| B | ARG40 |
| B | ARG91 |
| B | GLN92 |
| B | HIS93 |
| B | TYR96 |
| B | MG287 |
| B | HOH388 |
| B | HOH389 |
| B | HOH400 |
| B | HOH414 |
| B | HOH522 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 287 |
| Chain | Residue |
| B | HIS124 |
| B | ADP300 |
| B | HOH355 |
| B | HOH389 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE SO4 B 288 |
| Chain | Residue |
| B | ARG91 |
| B | ILE213 |
| B | SER214 |
| B | THR215 |
| B | GLY216 |
| B | GLY217 |
| B | THR218 |
| B | HOH332 |
| B | HOH468 |
| B | HOH474 |
| B | HOH510 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 289 |
| Chain | Residue |
| B | ARG7 |
| B | SER58 |
| B | HOH352 |
| B | HOH530 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 290 |
| Chain | Residue |
| B | LYS195 |
| B | ASN198 |
| B | LYS229 |
| B | HOH344 |
| B | HOH505 |
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 |
| B | ASP34 | |
| B | SER214 | |
| A | ASP34 | |
| A | 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 |
