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5F7X

Crystal structure of Mutant Q289L of adenosine/Methylthioadenosine phosphorylase from Schistosoma mansoni in complex with Tubercidin

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006166biological_processpurine ribonucleoside salvage
A0009116biological_processnucleoside metabolic process
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0016763molecular_functionpentosyltransferase activity
A0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
A0019509biological_processL-methionine salvage from methylthioadenosine
B0003824molecular_functioncatalytic activity
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006166biological_processpurine ribonucleoside salvage
B0009116biological_processnucleoside metabolic process
B0016740molecular_functiontransferase activity
B0016757molecular_functionglycosyltransferase activity
B0016763molecular_functionpentosyltransferase activity
B0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
B0019509biological_processL-methionine salvage from methylthioadenosine
C0003824molecular_functioncatalytic activity
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006166biological_processpurine ribonucleoside salvage
C0009116biological_processnucleoside metabolic process
C0016740molecular_functiontransferase activity
C0016757molecular_functionglycosyltransferase activity
C0016763molecular_functionpentosyltransferase activity
C0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
C0019509biological_processL-methionine salvage from methylthioadenosine
Functional Information from PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue TBN A 301
ChainResidue
APRO63
ASO4302
AHOH429
CHIS131
AALA88
ACYS89
AGLY90
AVAL204
AMET206
ATHR229
AASP230
AASP232

site_idAC2
Number of Residues7
Detailsbinding site for residue SO4 A 302
ChainResidue
AGLY11
ASER12
AARG54
AHIS55
AALA88
ATHR207
ATBN301

site_idAC3
Number of Residues14
Detailsbinding site for residue TBN B 301
ChainResidue
BPRO63
BALA88
BCYS89
BGLY90
BPHE187
BVAL204
BASN205
BMET206
BTHR229
BASP232
BSO4302
BHOH455
BHOH562
BHOH586

site_idAC4
Number of Residues9
Detailsbinding site for residue SO4 B 302
ChainResidue
BGLY11
BSER12
BARG54
BHIS55
BALA88
BASN205
BTHR207
BTBN301
BHOH525

site_idAC5
Number of Residues16
Detailsbinding site for residue TBN C 301
ChainResidue
BHIS131
CPRO63
CALA88
CCYS89
CGLY90
CPHE187
CVAL204
CASN205
CMET206
CTHR229
CASP232
CSO4302
CHOH480
CHOH481
CHOH537
CHOH613

site_idAC6
Number of Residues10
Detailsbinding site for residue SO4 C 302
ChainResidue
CGLY11
CSER12
CARG54
CHIS55
CASN87
CALA88
CASN205
CTHR207
CTBN301
CHOH494

Functional Information from PROSITE/UniProt
site_idPS01240
Number of Residues41
DetailsPNP_MTAP_2 Purine and other phosphorylases family 2 signature. LprhGkgHlIppseVnyrAn.VwAlkdlGcth.ILatNAcGSL
ChainResidueDetails
ALEU52-LEU92

237735

PDB entries from 2025-06-18

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