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4S2U

Crystal structure of the Phosphorybosylpyrophosphate synthetase from E. Coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0002189cellular_componentribose phosphate diphosphokinase complex
A0004749molecular_functionribose phosphate diphosphokinase activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006015biological_process5-phosphoribose 1-diphosphate biosynthetic process
A0006164biological_processpurine nucleotide biosynthetic process
A0009156biological_processribonucleoside monophosphate biosynthetic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0034214biological_processprotein hexamerization
A0042301molecular_functionphosphate ion binding
A0042802molecular_functionidentical protein binding
A0043531molecular_functionADP binding
A0044249biological_processcellular biosynthetic process
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 401
ChainResidue
AASP224
ATHR225
ATHR228

Functional Information from PROSITE/UniProt
site_idPS00103
Number of Residues13
DetailsPUR_PYR_PR_TRANSFER Purine/pyrimidine phosphoribosyl transferases signature. CVLVDDMIDTGgT
ChainResidueDetails
ACYS216-THR228

site_idPS00114
Number of Residues16
DetailsPRPP_SYNTHASE Phosphoribosyl pyrophosphate synthase signature. DLHAeQIQGFFdvPVD
ChainResidueDetails
AASP129-ASP144

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:7657655
ChainResidueDetails
ALYS194

site_idSWS_FT_FI2
Number of Residues7
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00583
ChainResidueDetails
AASP37
AARG96
AHIS131
AASP170
AARG196
AASP220
AASP224

219140

PDB entries from 2024-05-01

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