1BX3
EFFECTS OF COMMONLY USED CRYOPROTECTANTS ON GLYCOGEN PHOSPHORYLASE ACTIVITY AND STRUCTURE
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 PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE PLP A 999 |
Chain | Residue |
A | GLY134 |
A | GLY677 |
A | LYS680 |
A | HOH1017 |
A | HOH1025 |
A | HOH1028 |
A | HOH1041 |
A | HOH1044 |
A | HOH1110 |
A | HOH1146 |
A | TRP491 |
A | LYS568 |
A | LYS574 |
A | TYR648 |
A | ARG649 |
A | VAL650 |
A | GLY675 |
A | THR676 |
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 | ASP42 | |
A | ARG309 |
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 | CYS108 | |
A | CYS142 |
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 | TYR203 | |
A | TYR226 |
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 | SER513 | |
A | SER746 | |
A | SER747 |
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 | 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 | LYS680 | covalently attached |