3E3O
Glycogen phosphorylase R state-IMP complex
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 | 0008152 | biological_process | metabolic 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 |
A | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
A | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
B | 0000166 | molecular_function | nucleotide binding |
B | 0003824 | molecular_function | catalytic activity |
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 | 0008152 | biological_process | metabolic process |
B | 0008184 | molecular_function | glycogen phosphorylase activity |
B | 0016740 | molecular_function | transferase 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 | linear malto-oligosaccharide phosphorylase activity |
B | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
C | 0000166 | molecular_function | nucleotide binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
C | 0005737 | cellular_component | cytoplasm |
C | 0005975 | biological_process | carbohydrate metabolic process |
C | 0005977 | biological_process | glycogen metabolic process |
C | 0005980 | biological_process | glycogen catabolic process |
C | 0008152 | biological_process | metabolic process |
C | 0008184 | molecular_function | glycogen phosphorylase activity |
C | 0016740 | molecular_function | transferase activity |
C | 0016757 | molecular_function | glycosyltransferase activity |
C | 0030170 | molecular_function | pyridoxal phosphate binding |
C | 0098723 | cellular_component | skeletal muscle myofibril |
C | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
C | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
D | 0000166 | molecular_function | nucleotide binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
D | 0005737 | cellular_component | cytoplasm |
D | 0005975 | biological_process | carbohydrate metabolic process |
D | 0005977 | biological_process | glycogen metabolic process |
D | 0005980 | biological_process | glycogen catabolic process |
D | 0008152 | biological_process | metabolic process |
D | 0008184 | molecular_function | glycogen phosphorylase activity |
D | 0016740 | molecular_function | transferase activity |
D | 0016757 | molecular_function | glycosyltransferase activity |
D | 0030170 | molecular_function | pyridoxal phosphate binding |
D | 0098723 | cellular_component | skeletal muscle myofibril |
D | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
D | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 A 901 |
Chain | Residue |
A | GLY135 |
A | ARG569 |
A | TYR573 |
A | LYS574 |
A | LLP680 |
site_id | AC2 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE IMP A 920 |
Chain | Residue |
A | ARG310 |
A | HOH932 |
B | ASP42 |
B | ASN44 |
A | TRP67 |
A | GLN71 |
A | TYR75 |
A | ARG309 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 900 |
Chain | Residue |
A | SER14 |
A | ARG69 |
B | ARG43 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 901 |
Chain | Residue |
A | ARG43 |
B | SER14 |
B | ARG69 |
site_id | AC5 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 B 902 |
Chain | Residue |
B | GLY134 |
B | GLY135 |
B | ARG569 |
B | LYS574 |
site_id | AC6 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE IMP B 920 |
Chain | Residue |
A | ASP42 |
A | ASN44 |
B | TRP67 |
B | GLN71 |
B | TYR75 |
B | ARG309 |
B | ARG310 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 900 |
Chain | Residue |
C | SER14 |
C | ARG69 |
D | ARG43 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 C 901 |
Chain | Residue |
C | ARG569 |
C | LYS574 |
site_id | AC9 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE IMP C 920 |
Chain | Residue |
C | GLN71 |
C | TYR75 |
C | ARG309 |
C | ARG310 |
D | ASP42 |
D | ASN44 |
D | VAL45 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 900 |
Chain | Residue |
C | ARG43 |
D | SER14 |
D | ARG69 |
site_id | BC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE SO4 D 901 |
Chain | Residue |
D | GLY135 |
D | ARG569 |
D | LYS574 |
D | LLP680 |
site_id | BC3 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE IMP D 920 |
Chain | Residue |
C | ASP42 |
C | ASN44 |
C | VAL45 |
D | TRP67 |
D | GLN71 |
D | TYR75 |
D | ARG309 |
D | ARG310 |
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 | 8 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:P11217 |
Chain | Residue | Details |
A | ASP42 | |
A | ARG309 | |
B | ASP42 | |
B | ARG309 | |
C | ASP42 | |
C | ARG309 | |
D | ASP42 | |
D | ARG309 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:3616621 |
Chain | Residue | Details |
A | TYR75 | |
B | TYR75 | |
C | TYR75 | |
D | TYR75 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Involved in the association of subunits => ECO:0000303|PubMed:728424 |
Chain | Residue | Details |
A | CYS108 | |
A | CYS142 | |
B | CYS108 | |
B | CYS142 | |
C | CYS108 | |
C | CYS142 | |
D | CYS108 | |
D | CYS142 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424 |
Chain | Residue | Details |
A | TYR155 | |
B | TYR155 | |
C | TYR155 | |
D | TYR155 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:3015680 |
Chain | Residue | Details |
A | SER1 | |
B | SER1 | |
C | SER1 | |
D | SER1 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217 |
Chain | Residue | Details |
A | SER14 | |
B | SER14 | |
C | SER14 | |
D | SER14 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812 |
Chain | Residue | Details |
A | TYR203 | |
A | TYR226 | |
B | TYR203 | |
B | TYR226 | |
C | TYR203 | |
C | TYR226 | |
D | TYR203 | |
D | TYR226 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 |
Chain | Residue | Details |
A | SER429 | |
B | SER429 | |
C | SER429 | |
D | SER429 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 |
Chain | Residue | Details |
A | TYR472 | |
B | TYR472 | |
C | TYR472 | |
D | TYR472 |
site_id | SWS_FT_FI10 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812 |
Chain | Residue | Details |
A | SER513 | |
D | SER513 | |
D | SER746 | |
D | SER747 | |
A | SER746 | |
A | SER747 | |
B | SER513 | |
B | SER746 | |
B | SER747 | |
C | SER513 | |
C | SER746 | |
C | SER747 |
site_id | SWS_FT_FI11 |
Number of Residues | 4 |
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 | LLP680 | |
B | LLP680 | |
C | LLP680 | |
D | LLP680 |
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 | LLP680 | covalently attached |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 205 |
Chain | Residue | Details |
B | HIS377 | electrostatic stabiliser |
B | LYS568 | electrostatic stabiliser |
B | ARG569 | electrostatic stabiliser |
B | LYS574 | electrostatic stabiliser |
B | THR676 | electrostatic stabiliser |
B | LLP680 | covalently attached |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 205 |
Chain | Residue | Details |
C | HIS377 | electrostatic stabiliser |
C | LYS568 | electrostatic stabiliser |
C | ARG569 | electrostatic stabiliser |
C | LYS574 | electrostatic stabiliser |
C | THR676 | electrostatic stabiliser |
C | LLP680 | covalently attached |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 205 |
Chain | Residue | Details |
D | HIS377 | electrostatic stabiliser |
D | LYS568 | electrostatic stabiliser |
D | ARG569 | electrostatic stabiliser |
D | LYS574 | electrostatic stabiliser |
D | THR676 | electrostatic stabiliser |
D | LLP680 | covalently attached |