1Z8D
Crystal Structure of Human Muscle Glycogen Phosphorylase a with AMP and Glucose
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0005977 | biological_process | glycogen metabolic process |
| A | 0005980 | biological_process | glycogen catabolic process |
| A | 0008184 | molecular_function | glycogen phosphorylase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0102250 | molecular_function | obsolete linear malto-oligosaccharide phosphorylase activity |
| A | 0102499 | molecular_function | obsolete SHG alpha-glucan phosphorylase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00102 |
| Number of Residues | 13 |
| Details | PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN |
| Chain | Residue | Details |
| A | GLU672-ASN684 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16523484, ECO:0007744|PDB:1Z8D |
| Chain | Residue | Details |
| A | ASP42 | |
| A | TYR75 | |
| A | ARG309 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | SITE: Involved in the association of subunits => ECO:0000250|UniProtKB:P00489 |
| Chain | Residue | Details |
| A | CYS108 | |
| A | CYS142 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | SITE: May be involved in allosteric control => ECO:0000250|UniProtKB:P00489 |
| Chain | Residue | Details |
| A | TYR155 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P00489 |
| Chain | Residue | Details |
| A | SER1 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PHK; in form phosphorylase A => ECO:0000269|PubMed:1150650 |
| Chain | Residue | Details |
| A | SEP14 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812 |
| Chain | Residue | Details |
| A | TYR203 | |
| A | TYR226 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 |
| Chain | Residue | Details |
| A | SER429 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 |
| Chain | Residue | Details |
| A | TYR472 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812 |
| Chain | Residue | Details |
| A | SER513 | |
| A | SER746 | |
| A | SER747 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000250|UniProtKB:P00489 |
| Chain | Residue | Details |
| A | LLP680 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gpa |
| Chain | Residue | Details |
| A | ARG569 | |
| A | LYS568 | |
| A | THR676 | |
| A | LYS574 |
