1ZCY
apo form of a mutant of glycogenin in which Asp159 is replaced by Ser
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005634 | cellular_component | nucleus |
A | 0005737 | cellular_component | cytoplasm |
A | 0005978 | biological_process | glycogen biosynthetic process |
A | 0008466 | molecular_function | glycogenin glucosyltransferase activity |
A | 0016740 | molecular_function | transferase activity |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0030145 | molecular_function | manganese ion binding |
A | 0042803 | molecular_function | protein homodimerization activity |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 401 |
Chain | Residue |
A | ASP177 |
A | ILE178 |
A | HOH411 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | Binding 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Binding 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P46976","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"22226635","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3V91","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"15849187","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1ZCT","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Binding 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"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"10049511","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"N-acetylthreonine","evidences":[{"source":"UniProtKB","id":"P46976","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by PKA; in vitro","evidences":[{"source":"PubMed","id":"3151442","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | Glycosylation: {"description":"O-linked (Glc...) tyrosine","evidences":[{"source":"PubMed","id":"8143846","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ga8 |
Chain | Residue | Details |
A | ASP124 | |
A | GLN163 | |
A | ASN132 |