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1SD1

STRUCTURE OF HUMAN 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH FORMYCIN A

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
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
A0032259biological_processmethylation
A0033574biological_processresponse to testosterone
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues14
DetailsBINDING SITE FOR RESIDUE FMC A 1330
ChainResidue
ATHR18
AASP220
AASP222
AVAL236
AHOH1337
AHOH1361
AALA94
ACYS95
AGLY96
APHE177
AILE194
AASN195
AMET196
ATHR219

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 Residues6
DetailsBINDING:
ChainResidueDetails
ATHR18
AARG60
ATHR93
AMET196
ATHR197
AASP220

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Important for substrate specificity
ChainResidueDetails
ASER178
AVAL233

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:Q9CQ65
ChainResidueDetails
ALYS51

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1cg6
ChainResidueDetails
AASP220
AASP222

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 2025-06-11

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