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5EP8

X-Ray Structure of the Complex Pyrimidine-nucleoside phosphorylase from Bacillus subtilis with Sulfate Ion

Functional Information from GO Data
ChainGOidnamespacecontents
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0004850molecular_functionuridine phosphorylase activity
A0005829cellular_componentcytosol
A0006206biological_processpyrimidine nucleobase metabolic process
A0006213biological_processpyrimidine nucleoside metabolic process
A0009032molecular_functionthymidine phosphorylase activity
A0016154molecular_functionpyrimidine-nucleoside phosphorylase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0046872molecular_functionmetal ion binding
A0047847molecular_functiondeoxyuridine phosphorylase activity
B0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
B0004850molecular_functionuridine phosphorylase activity
B0005829cellular_componentcytosol
B0006206biological_processpyrimidine nucleobase metabolic process
B0006213biological_processpyrimidine nucleoside metabolic process
B0009032molecular_functionthymidine phosphorylase activity
B0016154molecular_functionpyrimidine-nucleoside phosphorylase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0046872molecular_functionmetal ion binding
B0047847molecular_functiondeoxyuridine phosphorylase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue SO4 A 501
ChainResidue
ALYS81
ATHR92
ALYS108
ASER110
ATHR120
AHOH607

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 B 501
ChainResidue
BLYS108
BSER110
BTHR120

site_idAC3
Number of Residues5
Detailsbinding site for residue NA B 502
ChainResidue
BGLY88
BTHR90
BLEU243
BALA246
BGLU255

Functional Information from PROSITE/UniProt
site_idPS00647
Number of Residues16
DetailsTHYMID_PHOSPHORYLASE Thymidine and pyrimidine-nucleoside phosphorylases signature. SGRGLghTGGTiDkLE
ChainResidueDetails
ASER110-GLU125

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P77836
ChainResidueDetails
ALYS81
AALA246
AGLU255
BLYS81
BGLY88
BTHR90
BTHR92
BLYS108
BTHR120
BARG168
BLYS187
AGLY88
BLEU243
BALA246
BGLU255
ATHR90
ATHR92
ALYS108
ATHR120
AARG168
ALYS187
ALEU243

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PDB entries from 2024-07-10

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