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1ZCY

apo form of a mutant of glycogenin in which Asp159 is replaced by Ser

Functional Information from GO Data
ChainGOidnamespacecontents
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005978biological_processglycogen biosynthetic process
A0008466molecular_functionglycogenin glucosyltransferase activity
A0016740molecular_functiontransferase activity
A0016757molecular_functionglycosyltransferase activity
A0030145molecular_functionmanganese ion binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 401
ChainResidue
AASP177
AILE178
AHOH411

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12051921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15849187","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22226635","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LL2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZDF","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZDG","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3V91","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12051921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15849187","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LL2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ZDG","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P46976","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"22226635","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V91","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15849187","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZCT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12051921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22226635","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1LL2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3V91","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"10049511","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"N-acetylthreonine","evidences":[{"source":"UniProtKB","id":"P46976","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by PKA; in vitro","evidences":[{"source":"PubMed","id":"3151442","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Glc...) tyrosine","evidences":[{"source":"PubMed","id":"8143846","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ga8
ChainResidueDetails
AASP124
AGLN163
AASN132

239803

PDB entries from 2025-08-06

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