1LL2
Crystal Structure of Rabbit Muscle Glycogenin Complexed with UDP-glucose and Manganese
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 | 4 |
Details | BINDING SITE FOR RESIDUE MN A 333 |
Chain | Residue |
A | ASP102 |
A | ASP104 |
A | HIS212 |
A | UPG334 |
site_id | AC2 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE UPG A 334 |
Chain | Residue |
A | ASP102 |
A | ALA103 |
A | ASP104 |
A | ASP125 |
A | ASN133 |
A | SER134 |
A | GLN164 |
A | HIS212 |
A | LEU214 |
A | GLY215 |
A | LYS218 |
A | MN333 |
A | HOH356 |
A | HOH375 |
A | HOH416 |
A | HOH459 |
A | HOH492 |
A | HOH493 |
A | HOH520 |
A | HOH582 |
A | LEU9 |
A | THR10 |
A | THR11 |
A | ASN12 |
A | TYR15 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 9 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDF, ECO:0007744|PDB:1ZDG, ECO:0007744|PDB:3V91 |
Chain | Residue | Details |
A | LEU9 | |
A | THR11 | |
A | TYR15 | |
A | ASP102 | |
A | ALA103 | |
A | ASP104 | |
A | ASN133 | |
A | GLN164 | |
A | LYS218 |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:15849187, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:1ZDG |
Chain | Residue | Details |
A | ASN12 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P46976 |
Chain | Residue | Details |
A | ARG77 | |
A | LYS86 | |
A | ASP160 | |
A | ASP163 |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:22226635, ECO:0007744|PDB:3V91 |
Chain | Residue | Details |
A | SER134 |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15849187, ECO:0007744|PDB:1ZCT |
Chain | Residue | Details |
A | HIS212 |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | BINDING: BINDING => ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:22226635, ECO:0007744|PDB:1LL2, ECO:0007744|PDB:3V91 |
Chain | Residue | Details |
A | GLY215 |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | SITE: Important for catalytic activity => ECO:0000269|PubMed:10049511 |
Chain | Residue | Details |
A | LYS86 |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | MOD_RES: N-acetylthreonine => ECO:0000250|UniProtKB:P46976 |
Chain | Residue | Details |
A | THR2 |
site_id | SWS_FT_FI9 |
Number of Residues | 1 |
Details | MOD_RES: Phosphoserine; by PKA; in vitro => ECO:0000269|PubMed:3151442 |
Chain | Residue | Details |
A | SER44 |
site_id | SWS_FT_FI10 |
Number of Residues | 1 |
Details | CARBOHYD: O-linked (Glc...) tyrosine => ECO:0000269|PubMed:8143846 |
Chain | Residue | Details |
A | TYR195 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ga8 |
Chain | Residue | Details |
A | GLN164 | |
A | ASN133 | |
A | ASP125 |