5SUL
Inhibited state structure of yGsy2p
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004373 | molecular_function | glycogen (starch) synthase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005978 | biological_process | glycogen biosynthetic process |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0140678 | molecular_function | molecular function inhibitor activity |
| B | 0004373 | molecular_function | glycogen (starch) synthase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005978 | biological_process | glycogen biosynthetic process |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0140678 | molecular_function | molecular function inhibitor activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | binding site for residue UDP A 801 |
| Chain | Residue |
| A | GLY319 |
| A | GLU517 |
| A | ARG320 |
| A | LYS326 |
| A | PHE480 |
| A | LEU481 |
| A | TYR492 |
| A | GLY512 |
| A | TYR513 |
| A | THR514 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue U5P B 801 |
| Chain | Residue |
| B | GLY319 |
| B | ARG320 |
| B | LYS326 |
| B | PHE480 |
| B | LEU481 |
| B | TYR492 |
| B | TYR513 |
| B | GLU517 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| A | ARG20 | |
| B | ARG20 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0000255 |
| Chain | Residue | Details |
| A | SER159 | |
| A | SER363 | |
| B | SER159 | |
| B | SER363 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | SER467 | |
| B | SER467 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
| Chain | Residue | Details |
| A | SER651 | |
| B | SER651 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PHO85 => ECO:0000269|PubMed:9584169, ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | SER655 | |
| B | SER655 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by PKA => ECO:0000255 |
| Chain | Residue | Details |
| A | SER661 | |
| A | SER663 | |
| B | SER661 | |
| B | SER663 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine; by PHO85 => ECO:0000269|PubMed:9584169 |
| Chain | Residue | Details |
| A | THR668 | |
| B | THR668 |
