5LRF
Crystal structure of Glycogen Phosphorylase b in complex with KS389
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 | 18 |
| Details | binding site for residue KS3 A 901 |
| Chain | Residue |
| A | GLU88 |
| A | TYR573 |
| A | GLU672 |
| A | ALA673 |
| A | SER674 |
| A | GLY675 |
| A | HOH1081 |
| A | HOH1126 |
| A | HOH1154 |
| A | HOH1161 |
| A | LEU136 |
| A | ASN282 |
| A | ASN284 |
| A | PHE285 |
| A | HIS341 |
| A | HIS377 |
| A | ALA383 |
| A | ASN484 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue KS3 A 902 |
| Chain | Residue |
| A | PHE37 |
| A | THR38 |
| A | VAL40 |
| A | ARG60 |
| A | PRO188 |
| A | TRP189 |
| A | GLU190 |
| A | LYS191 |
| A | ALA192 |
| A | PRO229 |
| A | HOH1001 |
| A | HOH1007 |
| A | HOH1089 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 903 |
| Chain | Residue |
| A | ARG309 |
| A | ARG310 |
| A | DMS904 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | binding site for residue DMS A 904 |
| Chain | Residue |
| A | VAL45 |
| A | TYR75 |
| A | DMS903 |
| A | HOH1313 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue PLP A 905 |
| Chain | Residue |
| A | GLY134 |
| A | LYS568 |
| A | LYS574 |
| A | TYR648 |
| A | ARG649 |
| A | VAL650 |
| A | GLY675 |
| A | THR676 |
| A | GLY677 |
| A | LYS680 |
| A | HOH1031 |
| A | HOH1048 |
| A | HOH1055 |
| A | HOH1081 |
| A | HOH1174 |
| A | HOH1218 |
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 |
