3DAH
2.3 A crystal structure of ribose-phosphate pyrophosphokinase from Burkholderia pseudomallei
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
| A | 0009165 | biological_process | nucleotide biosynthetic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0044249 | biological_process | cellular biosynthetic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| 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 | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
| B | 0009165 | biological_process | nucleotide biosynthetic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0044249 | biological_process | cellular biosynthetic process |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004749 | molecular_function | ribose phosphate diphosphokinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
| C | 0009156 | biological_process | ribonucleoside monophosphate biosynthetic process |
| C | 0009165 | biological_process | nucleotide biosynthetic process |
| C | 0016301 | molecular_function | kinase activity |
| C | 0044249 | biological_process | cellular biosynthetic process |
| C | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 319 |
| Chain | Residue |
| A | ASN50 |
| A | ARG52 |
| A | ARG108 |
| B | SER310 |
| B | MET312 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 319 |
| Chain | Residue |
| C | ARG52 |
| A | SER310 |
| A | MET312 |
| B | ARG108 |
| C | ASN50 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 B 320 |
| Chain | Residue |
| B | ASP226 |
| B | THR227 |
| B | ALA228 |
| B | GLY229 |
| B | THR230 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 A 320 |
| Chain | Residue |
| A | ASP226 |
| A | THR227 |
| A | ALA228 |
| A | GLY229 |
| A | THR230 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PO4 C 319 |
| Chain | Residue |
| C | ASP226 |
| C | THR227 |
| C | ALA228 |
| C | GLY229 |
| C | THR230 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE PO4 B 321 |
| Chain | Residue |
| B | ARG52 |
| C | ARG108 |
| C | ARG304 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 B 322 |
| Chain | Residue |
| B | GLU49 |
| B | ASN50 |
| B | ARG262 |
| C | ARG108 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AMP A 401 |
| Chain | Residue |
| A | PHE38 |
| A | ASP40 |
| A | GLU42 |
| A | ARG99 |
| A | GLN100 |
| A | HIS134 |
| site_id | AC9 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AMP B 401 |
| Chain | Residue |
| B | PHE38 |
| B | ASP40 |
| B | GLU42 |
| C | ARG99 |
| C | GLN100 |
| C | ARG102 |
| C | PRO104 |
| C | HIS134 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE AMP B 402 |
| Chain | Residue |
| B | ARG99 |
| B | GLN100 |
| B | ARG102 |
| B | HIS134 |
| C | PHE38 |
| C | ASP40 |
| C | GLU42 |
Functional Information from PROSITE/UniProt
| site_id | PS00103 |
| Number of Residues | 13 |
| Details | PUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. CVIMDDMVDTAgT |
| Chain | Residue | Details |
| A | CYS218-THR230 |
| site_id | PS00114 |
| Number of Residues | 16 |
| Details | PRPP_SYNTHASE Phosphoribosyl pyrophosphate synthase signature. DLHAdQIQGFFdiPVD |
| Chain | Residue | Details |
| A | ASP132-ASP147 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00583 |
| Chain | Residue | Details |
| A | LYS196 | |
| B | LYS196 | |
| C | LYS196 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 15 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583 |
| Chain | Residue | Details |
| A | ASP40 | |
| B | ASP222 | |
| C | ASP40 | |
| C | HIS134 | |
| C | ASP173 | |
| C | ARG198 | |
| C | ASP222 | |
| A | HIS134 | |
| A | ASP173 | |
| A | ARG198 | |
| A | ASP222 | |
| B | ASP40 | |
| B | HIS134 | |
| B | ASP173 | |
| B | ARG198 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:23382856, ECO:0007744|PDB:3DAH |
| Chain | Residue | Details |
| A | ARG99 | |
| B | ARG99 | |
| C | ARG99 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:23382856, ECO:0007744|PDB:3DAH |
| Chain | Residue | Details |
| A | ASP226 | |
| B | ASP226 | |
| C | ASP226 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1l1r |
| Chain | Residue | Details |
| B | GLY175 | |
| B | GLU212 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1l1r |
| Chain | Residue | Details |
| C | GLY175 | |
| C | GLU212 |
