1XL1
Kinetic and crystallographic studies on 2-(beta-D-glucopyranosyl)-5-methyl-1,3,4-oxadiazole,-benzothiazole, and-benzimidazole, inhibitors of muscle glycogen phosphorylase b. Evidence for a new binding site.
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 | 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 | 0016757 | molecular_function | glycosyltransferase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0098723 | cellular_component | skeletal muscle myofibril |
| 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 | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11217 |
| Chain | Residue | Details |
| A | ARG43 | |
| A | ARG310 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:3616621 |
| Chain | Residue | Details |
| A | GLU76 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Involved in the association of subunits => ECO:0000303|PubMed:728424 |
| Chain | Residue | Details |
| A | ASP109 | |
| A | PHE143 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | SITE: Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 |
| Chain | Residue | Details |
| A | GLY156 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:3015680 |
| Chain | Residue | Details |
| A | ARG2 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 |
| Chain | Residue | Details |
| A | VAL15 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812 |
| Chain | Residue | Details |
| A | GLY204 | |
| A | ASP227 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 |
| Chain | Residue | Details |
| A | LEU430 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 |
| Chain | Residue | Details |
| A | GLU473 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812 |
| Chain | Residue | Details |
| A | ASP514 | |
| A | SER747 | |
| A | GLY748 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7500360, ECO:0000269|PubMed:8976550, ECO:0007744|PDB:2PRI, ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD, ECO:0007744|PDB:2SKE |
| Chain | Residue | Details |
| A | PHE681 |
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 | THR378 | electrostatic stabiliser |
| A | ARG569 | electrostatic stabiliser |
| A | ILE570 | electrostatic stabiliser |
| A | ARG575 | electrostatic stabiliser |
| A | GLY677 | electrostatic stabiliser |
| A | PHE681 | covalently attached |
