6F3R
The crystal structure of Glycogen Phosphorylase in complex with 10c
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 PDB Data
site_id | AC1 |
Number of Residues | 17 |
Details | binding site for residue PLP A 901 |
Chain | Residue |
A | GLY134 |
A | GLY677 |
A | LYS680 |
A | HOH1019 |
A | HOH1034 |
A | HOH1072 |
A | HOH1080 |
A | HOH1114 |
A | HOH1180 |
A | GLY135 |
A | LYS568 |
A | LYS574 |
A | TYR648 |
A | ARG649 |
A | VAL650 |
A | GLY675 |
A | THR676 |
site_id | AC2 |
Number of Residues | 17 |
Details | binding site for residue CKZ A 902 |
Chain | Residue |
A | GLU88 |
A | LEU136 |
A | ASN282 |
A | ASN284 |
A | PHE285 |
A | ARG292 |
A | HIS377 |
A | ASN484 |
A | TYR573 |
A | GLU672 |
A | ALA673 |
A | SER674 |
A | GLY675 |
A | HOH1034 |
A | HOH1088 |
A | HOH1147 |
A | HOH1184 |
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 | 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 | LYS680 | covalently attached |