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5MP7

Crystal structure of phosphoribosylpyrophosphate synthetase from Mycobacterium smegmatis

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0004749molecular_functionribose phosphate diphosphokinase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0006015biological_process5-phosphoribose 1-diphosphate biosynthetic process
A0009156biological_processribonucleoside monophosphate biosynthetic process
A0009165biological_processnucleotide biosynthetic process
A0016301molecular_functionkinase activity
A0044249biological_processcellular biosynthetic process
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0004749molecular_functionribose phosphate diphosphokinase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0006015biological_process5-phosphoribose 1-diphosphate biosynthetic process
B0009156biological_processribonucleoside monophosphate biosynthetic process
B0009165biological_processnucleotide biosynthetic process
B0016301molecular_functionkinase activity
B0044249biological_processcellular biosynthetic process
B0046872molecular_functionmetal ion binding
C0000287molecular_functionmagnesium ion binding
C0004749molecular_functionribose phosphate diphosphokinase activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0006015biological_process5-phosphoribose 1-diphosphate biosynthetic process
C0009156biological_processribonucleoside monophosphate biosynthetic process
C0009165biological_processnucleotide biosynthetic process
C0016301molecular_functionkinase activity
C0044249biological_processcellular biosynthetic process
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ACT A 401
ChainResidue
AASP234
ATHR235
AGLY236
AGLY237
ATHR238

site_idAC2
Number of Residues5
Detailsbinding site for residue ACT C 401
ChainResidue
CTHR238
BGLN269
CASP234
CTHR235
CGLY236

site_idAC3
Number of Residues3
Detailsbinding site for residue ACT B 401
ChainResidue
BASP234
BTHR235
BTHR238

site_idAC4
Number of Residues13
Detailsbinding site for Di-peptide ARG B 181 and ASP B 231
ChainResidue
BHIS138
BSER176
BASP178
BSER179
BGLY180
BVAL182
BARG183
BVAL184
BALA185
BASP230
BMET232
BTHR259
BHIS260

Functional Information from PROSITE/UniProt
site_idPS00114
Number of Residues16
DetailsPRPP_SYNTHASE Phosphoribosyl pyrophosphate synthase signature. DLHTdQIQGFFdgPVD
ChainResidueDetails
AASP136-ASP151

site_idPS00144
Number of Residues9
DetailsASN_GLN_ASE_1 Asparaginase / glutaminase active site signature 1. MiDTGGTIA
ChainResidueDetails
AMET232-ALA240

222624

PDB entries from 2024-07-17

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