2GPN
100 K STRUCTURE OF GLYCOGEN PHOSPHORYLASE AT 2.0 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 0016740 | molecular_function | transferase activity |
| A | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0098723 | cellular_component | skeletal muscle myofibril |
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 | 1 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"3616621","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Involved in the association of subunits","evidences":[{"source":"PubMed","id":"728424","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Can be labeled by an AMP analog; may be involved in allosteric regulation","evidences":[{"source":"PubMed","id":"728424","evidenceCode":"ECO:0000303"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PHK; in form phosphorylase A","evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"7500360","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8976550","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PRI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKE","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
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 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 205 |
| Chain | Residue | Details |
| A | HIS377 | electrostatic stabiliser |
| A | LYS568 | electrostatic stabiliser |
| A | ARG569 | electrostatic stabiliser |
| A | LYS574 | electrostatic stabiliser |
| A | THR676 | electrostatic stabiliser |
| A | LLP680 | covalently attached |
