2IEG
Crystal structure of rabbit muscle glycogen phosphorylase in complex with 3,4-dihydro-2-quinolone
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 |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005975 | biological_process | carbohydrate metabolic process |
| B | 0005977 | biological_process | glycogen metabolic process |
| B | 0005980 | biological_process | glycogen catabolic process |
| B | 0008184 | molecular_function | glycogen phosphorylase activity |
| B | 0016757 | molecular_function | glycosyltransferase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0098723 | cellular_component | skeletal muscle myofibril |
| B | 0102250 | molecular_function | obsolete linear malto-oligosaccharide phosphorylase activity |
| B | 0102499 | molecular_function | obsolete SHG alpha-glucan phosphorylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLR A 903 |
| Chain | Residue |
| A | GLY134 |
| A | LYS680 |
| A | HOH925 |
| A | HOH936 |
| A | HOH951 |
| A | HOH959 |
| A | HOH988 |
| A | HOH1266 |
| A | LYS568 |
| A | LYS574 |
| A | TYR648 |
| A | ARG649 |
| A | VAL650 |
| A | GLY675 |
| A | THR676 |
| A | GLY677 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PLR B 904 |
| Chain | Residue |
| B | GLY134 |
| B | TRP491 |
| B | LYS568 |
| B | LYS574 |
| B | TYR648 |
| B | ARG649 |
| B | VAL650 |
| B | GLY675 |
| B | THR676 |
| B | GLY677 |
| B | LYS680 |
| B | HOH908 |
| B | HOH936 |
| B | HOH961 |
| B | HOH997 |
| B | HOH1007 |
| B | HOH1058 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE FRY A 901 |
| Chain | Residue |
| A | ARG60 |
| A | TRP67 |
| A | PRO188 |
| A | GLU190 |
| A | LYS191 |
| A | ALA192 |
| A | HOH1104 |
| A | HOH1179 |
| B | THR38 |
| B | LEU39 |
| B | VAL40 |
| B | HIS57 |
| B | TYR185 |
| B | GLY186 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE FRY B 902 |
| Chain | Residue |
| A | THR38 |
| A | LEU39 |
| A | VAL40 |
| A | PHE53 |
| A | HIS57 |
| A | TYR185 |
| A | GLY186 |
| B | ARG60 |
| B | PRO188 |
| B | GLU190 |
| B | LYS191 |
| B | ALA192 |
| B | HOH1107 |
| B | HOH1126 |
| B | HOH1230 |
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 | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11217 |
| Chain | Residue | Details |
| A | ARG43 | |
| A | ARG310 | |
| B | ARG43 | |
| B | ARG310 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:3616621 |
| Chain | Residue | Details |
| A | GLU76 | |
| B | GLU76 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Involved in the association of subunits => ECO:0000303|PubMed:728424 |
| Chain | Residue | Details |
| A | ASP109 | |
| A | PHE143 | |
| B | ASP109 | |
| B | PHE143 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 |
| Chain | Residue | Details |
| A | GLY156 | |
| B | GLY156 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:3015680 |
| Chain | Residue | Details |
| A | ARG2 | |
| B | ARG2 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 |
| Chain | Residue | Details |
| A | VAL15 | |
| B | VAL15 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812 |
| Chain | Residue | Details |
| A | GLY204 | |
| A | ASP227 | |
| B | GLY204 | |
| B | ASP227 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 |
| Chain | Residue | Details |
| A | LEU430 | |
| B | LEU430 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 |
| Chain | Residue | Details |
| A | GLU473 | |
| B | GLU473 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812 |
| Chain | Residue | Details |
| A | ASP514 | |
| A | SER747 | |
| A | GLY748 | |
| B | ASP514 | |
| B | SER747 | |
| B | GLY748 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 2 |
| 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 | |
| B | 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 | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gpa |
| Chain | Residue | Details |
| B | ARG569 | |
| B | LYS568 | |
| B | THR676 | |
| B | 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 |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 205 |
| Chain | Residue | Details |
| B | THR378 | electrostatic stabiliser |
| B | ARG569 | electrostatic stabiliser |
| B | ILE570 | electrostatic stabiliser |
| B | ARG575 | electrostatic stabiliser |
| B | GLY677 | electrostatic stabiliser |
| B | PHE681 | covalently attached |
