5JTT
Crystal structure of GPb in complex with 8a
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 | linear malto-oligosaccharide phosphorylase activity |
| A | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
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 | HOH1026 |
| A | HOH1030 |
| A | HOH1044 |
| A | HOH1076 |
| A | HOH1147 |
| A | HOH1186 |
| A | GLY135 |
| A | LYS568 |
| A | LYS574 |
| A | TYR648 |
| A | ARG649 |
| A | VAL650 |
| A | GLY675 |
| A | THR676 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue 6MY A 902 |
| Chain | Residue |
| A | GLU88 |
| A | LEU136 |
| A | ASN282 |
| A | ASN284 |
| A | HIS341 |
| A | HIS377 |
| A | ASN484 |
| A | TYR573 |
| A | GLU672 |
| A | ALA673 |
| A | SER674 |
| A | GLY675 |
| A | HOH1044 |
| A | HOH1125 |
| A | HOH1148 |
| A | HOH1207 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue DMS A 903 |
| Chain | Residue |
| A | ARG309 |
| A | ARG310 |
| A | HOH1319 |
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 | ARG309 | |
| A | ASP42 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:3616621 |
| Chain | Residue | Details |
| A | TYR75 |
| 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 | CYS142 | |
| A | CYS108 |
| 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 | TYR155 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:3015680 |
| Chain | Residue | Details |
| A | SER1 |
| 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 | SER14 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812 |
| Chain | Residue | Details |
| A | TYR226 | |
| A | TYR203 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 |
| Chain | Residue | Details |
| A | SER429 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 |
| Chain | Residue | Details |
| A | TYR472 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 3 |
| Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812 |
| Chain | Residue | Details |
| A | SER746 | |
| A | SER747 | |
| A | SER513 |
| 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 | LYS680 |
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 |
