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5TC7

Crystal structure of human 5'-deoxy-5'-methylthioadenosine phosphorylase in complex with 5'-methylthiotubercidin at 1.75 angstrom

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006139biological_processnucleobase-containing compound metabolic process
A0006166biological_processpurine ribonucleoside salvage
A0006738biological_processnicotinamide riboside catabolic process
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
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PO4 A 301
ChainResidue
AGLY17
ATHR18
AARG60
AHIS61
ATHR93
AALA94
ATHR197
AMTH304

site_idAC2
Number of Residues6
Detailsbinding site for residue PO4 A 302
ChainResidue
ATHR118
ATHR118
AMET119
AMET119
AMET119
ATHR118

site_idAC3
Number of Residues6
Detailsbinding site for residue PO4 A 303
ChainResidue
AARG99
AGLU100
AGLU101
AARG187
ATRP224
AHOH468

site_idAC4
Number of Residues13
Detailsbinding site for residue MTH A 304
ChainResidue
APRO69
AALA94
ACYS95
AGLY96
APHE177
AASN195
AMET196
ATHR219
AASP220
AASP222
APO4301
AHOH413
AHOH507

site_idAC5
Number of Residues3
Detailsbinding site for residue CL A 305
ChainResidue
AARG116
AARG116
AARG116

Functional Information from PROSITE/UniProt
site_idPS01240
Number of Residues41
DetailsPNP_MTAP_2 Purine and other phosphorylases family 2 signature. LarhGrqHtImpskVnyqAn.IwAlkeeGcth.VIvtTAcGSL
ChainResidueDetails
ALEU58-LEU98

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsSite: {"description":"Important for substrate specificity"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQ65","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 244
ChainResidueDetails
AASP220hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AASP222electrostatic stabiliser

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PDB entries from 2025-12-17

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