2QRQ
Glycogen Phosphorylase b in complex with (1R)-3'-(4-methylphenyl)-spiro[1,5-anhydro-D-glucitol-1,5'-isoxazoline]
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 | 15 |
| Details | BINDING SITE FOR RESIDUE S13 A 998 |
| Chain | Residue |
| A | GLU88 |
| A | SER674 |
| A | GLY675 |
| A | HOH1042 |
| A | HOH1169 |
| A | HOH1456 |
| A | HOH1893 |
| A | LEU136 |
| A | ASP283 |
| A | HIS341 |
| A | HIS377 |
| A | ASN484 |
| A | TYR573 |
| A | GLU672 |
| A | ALA673 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 931 |
| Chain | Residue |
| A | TRP67 |
| A | ILE68 |
| A | ARG193 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS A 936 |
| Chain | Residue |
| A | GLN219 |
| A | LYS294 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS A 937 |
| Chain | Residue |
| A | HIS201 |
| A | TRP215 |
| A | ARG351 |
| A | LEU356 |
| A | HOH1066 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS A 938 |
| Chain | Residue |
| A | ARG519 |
| A | GLU701 |
| A | GLU702 |
| A | ALA703 |
| A | HOH1154 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS A 939 |
| Chain | Residue |
| A | GLU706 |
| A | PHE708 |
| A | PHE709 |
| A | ARG786 |
| A | HOH1242 |
| A | HOH1761 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS A 940 |
| Chain | Residue |
| A | ARG66 |
| A | LEU102 |
| A | ARG234 |
| A | ASN236 |
| A | ARG833 |
| A | HOH1104 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DMS A 942 |
| Chain | Residue |
| A | TYR548 |
| A | GLU552 |
| A | TYR553 |
| A | ARG649 |
| A | HOH1321 |
| A | HOH1713 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS A 945 |
| Chain | Residue |
| A | GLN264 |
| A | LEU267 |
| A | ASP268 |
| A | ASN270 |
| A | ASN274 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE DMS A 946 |
| Chain | Residue |
| A | TYR553 |
| A | PHE644 |
| A | LEU645 |
| A | GLU646 |
| A | HOH1120 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE DMS A 947 |
| Chain | Residue |
| A | HIS767 |
| A | ASP769 |
| site_id | BC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 948 |
| Chain | Residue |
| A | THR197 |
| A | LEU222 |
| A | HOH1737 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 953 |
| Chain | Residue |
| A | ALA535 |
| A | PRO794 |
| A | THR798 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE DMS A 955 |
| Chain | Residue |
| A | ARG427 |
| A | HIS443 |
| A | THR466 |
| A | ILE467 |
| A | PHE468 |
| A | LYS469 |
| A | ASP470 |
| A | PHE471 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 956 |
| Chain | Residue |
| A | HIS36 |
| A | PHE37 |
| A | HOH1462 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DMS A 958 |
| Chain | Residue |
| A | GLN408 |
| A | LEU411 |
| A | ASN412 |
| A | ASN595 |
| site_id | BC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE DMS A 972 |
| Chain | Residue |
| A | LEU271 |
| A | ASN274 |
| A | HOH1603 |
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 |
