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9S7V

Structure of glycogen phosphorylase - dimeric form - from Escherichia coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0005980biological_processglycogen catabolic process
A0008184molecular_functionglycogen phosphorylase activity
A0018106biological_processpeptidyl-histidine phosphorylation
A0030170molecular_functionpyridoxal phosphate binding
A0042803molecular_functionprotein homodimerization activity
B0004645molecular_function1,4-alpha-oligoglucan phosphorylase activity
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005980biological_processglycogen catabolic process
B0008184molecular_functionglycogen phosphorylase activity
B0018106biological_processpeptidyl-histidine phosphorylation
B0030170molecular_functionpyridoxal phosphate binding
B0042803molecular_functionprotein homodimerization activity
Functional Information from PROSITE/UniProt
site_idPS00102
Number of Residues13
DetailsPHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtSnMKfaLN
ChainResidueDetails
AGLU654-ASN666

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsModified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2026-07-22

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