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1CG6

STRUCTURE OF HUMAN 5'-DEOXY-5'-METHYLTHIOADENOSINE PHOSPHORYLASE COMPLEXED WITH 5'-DEOXY-5'-METHYLTHIOADENOSINE AND SULFATE AT 1.7 A RESOLUTION

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
A0006738biological_processnicotinamide riboside catabolic process
A0009116biological_processnucleoside metabolic process
A0016763molecular_functionpentosyltransferase activity
A0017061molecular_functionS-methyl-5-thioadenosine phosphorylase activity
A0033353biological_processL-methionine cycle
A0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 295
ChainResidue
AGLY17
ATHR18
AARG60
AHIS61
ATHR93
AALA94
ATHR197
AMTA292

site_idAC2
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MTA A 292
ChainResidue
ACYS95
AGLY96
APHE177
AASN195
AMET196
ATHR219
AASP220
AASP222
ASO4295
AHOH305
AALA94

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 Residues1
DetailsActive site: {"description":"Proton donor/acceptor","evidences":[{"source":"PubMed","id":"10404592","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CG6","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15122881","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1K27","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10404592","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CB0","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsSite: {"description":"Important for substrate specificity","evidences":[{"source":"PubMed","id":"10404592","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQ65","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Detailsa catalytic site defined by CSA, PubMed 10404592
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 2026-07-01

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