1LL3
Crystal Structure of Rabbit Muscle Glycogenin
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 |
| A | 0160249 | biological_process | glycogen biosynthetic process via UDP-glucose |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 333 |
| Chain | Residue |
| A | GLU117 |
| A | GLU118 |
| A | LEU119 |
| A | PHE170 |
| A | SER172 |
| A | LYS180 |
| A | HOH342 |
| A | HOH356 |
| A | HOH367 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 334 |
| Chain | Residue |
| A | TRP127 |
| A | ASP129 |
| A | CYS130 |
| A | ASN171 |
| A | PHE203 |
| A | HOH349 |
| A | HOH357 |
| A | HOH452 |
| A | HOH510 |
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 |
