1GPA
STRUCTURAL MECHANISM FOR GLYCOGEN PHOSPHORYLASE CONTROL BY PHOSPHORYLATION AND AMP
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 |
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 | linear malto-oligosaccharide phosphorylase activity |
B | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
C | 0000166 | molecular_function | nucleotide binding |
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 | 0008184 | molecular_function | glycogen phosphorylase 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 | 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 | 0008184 | molecular_function | glycogen phosphorylase 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 | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 901 |
Chain | Residue |
A | ARG569 |
A | TYR573 |
A | LYS574 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 A 902 |
Chain | Residue |
A | ARG242 |
A | ARG310 |
site_id | AC3 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE SO4 B 901 |
Chain | Residue |
B | PLP999 |
B | GLY135 |
B | ARG569 |
B | TYR573 |
B | LYS574 |
site_id | AC4 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 B 902 |
Chain | Residue |
B | ARG242 |
B | ARG310 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 901 |
Chain | Residue |
C | ARG569 |
C | TYR573 |
C | LYS574 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 C 902 |
Chain | Residue |
C | TYR155 |
C | ARG242 |
C | ARG310 |
site_id | AC7 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 D 901 |
Chain | Residue |
D | ARG569 |
D | TYR573 |
D | LYS574 |
site_id | AC8 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE SO4 D 902 |
Chain | Residue |
D | ARG242 |
D | ARG310 |
site_id | AC9 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PLP A 999 |
Chain | Residue |
A | ARG138 |
A | TRP491 |
A | LYS568 |
A | TYR648 |
A | ARG649 |
A | VAL650 |
A | ALA653 |
A | GLY675 |
A | THR676 |
A | GLY677 |
A | LYS680 |
site_id | BC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE PLP B 999 |
Chain | Residue |
B | TRP491 |
B | LYS568 |
B | LYS574 |
B | TYR648 |
B | ARG649 |
B | ALA653 |
B | GLY675 |
B | THR676 |
B | GLY677 |
B | LYS680 |
B | SO4901 |
site_id | BC2 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PLP C 999 |
Chain | Residue |
C | ARG138 |
C | TRP491 |
C | LYS568 |
C | TYR648 |
C | ARG649 |
C | VAL650 |
C | GLY675 |
C | THR676 |
C | GLY677 |
C | LYS680 |
site_id | BC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE PLP D 999 |
Chain | Residue |
D | TYR90 |
D | ARG138 |
D | TRP491 |
D | LYS568 |
D | TYR648 |
D | ARG649 |
D | VAL650 |
D | THR676 |
D | GLY677 |
D | LYS680 |
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 | ARG43 | |
A | ARG310 | |
B | ARG43 | |
B | ARG310 | |
C | ARG43 | |
C | ARG310 | |
D | ARG43 | |
D | ARG310 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:3616621 |
Chain | Residue | Details |
A | GLU76 | |
B | GLU76 | |
C | GLU76 | |
D | GLU76 |
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 | ASP109 | |
A | PHE143 | |
B | ASP109 | |
B | PHE143 | |
C | ASP109 | |
C | PHE143 | |
D | ASP109 | |
D | PHE143 |
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 | GLY156 | |
B | GLY156 | |
C | GLY156 | |
D | GLY156 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:3015680 |
Chain | Residue | Details |
A | ARG2 | |
B | ARG2 | |
C | ARG2 | |
D | ARG2 |
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 | VAL15 | |
B | VAL15 | |
C | VAL15 | |
D | VAL15 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09812 |
Chain | Residue | Details |
A | GLY204 | |
A | ASP227 | |
B | GLY204 | |
B | ASP227 | |
C | GLY204 | |
C | ASP227 | |
D | GLY204 | |
D | ASP227 |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3 |
Chain | Residue | Details |
A | LEU430 | |
B | LEU430 | |
C | LEU430 | |
D | LEU430 |
site_id | SWS_FT_FI9 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3 |
Chain | Residue | Details |
A | GLU473 | |
B | GLU473 | |
C | GLU473 | |
D | GLU473 |
site_id | SWS_FT_FI10 |
Number of Residues | 12 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09812 |
Chain | Residue | Details |
A | ASP514 | |
D | ASP514 | |
D | SER747 | |
D | GLY748 | |
A | SER747 | |
A | GLY748 | |
B | ASP514 | |
B | SER747 | |
B | GLY748 | |
C | ASP514 | |
C | SER747 | |
C | GLY748 |
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 | PHE681 | |
B | PHE681 | |
C | PHE681 | |
D | PHE681 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 1900534, 6425278, 11886794, 15272305, 12460107 |
Chain | Residue | Details |
A | ARG569 | |
A | LYS568 | |
A | THR676 | |
A | LYS574 |
site_id | CSA2 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 1900534, 6425278, 11886794, 15272305, 12460107 |
Chain | Residue | Details |
B | ARG569 | |
B | LYS568 | |
B | THR676 | |
B | LYS574 |
site_id | CSA3 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 1900534, 6425278, 11886794, 15272305, 12460107 |
Chain | Residue | Details |
C | ARG569 | |
C | LYS568 | |
C | THR676 | |
C | LYS574 |
site_id | CSA4 |
Number of Residues | 4 |
Details | a catalytic site defined by CSA, PubMed 1900534, 6425278, 11886794, 15272305, 12460107 |
Chain | Residue | Details |
D | ARG569 | |
D | LYS568 | |
D | THR676 | |
D | 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 |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 205 |
Chain | Residue | Details |
C | THR378 | electrostatic stabiliser |
C | ARG569 | electrostatic stabiliser |
C | ILE570 | electrostatic stabiliser |
C | ARG575 | electrostatic stabiliser |
C | GLY677 | electrostatic stabiliser |
C | PHE681 | covalently attached |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 205 |
Chain | Residue | Details |
D | THR378 | electrostatic stabiliser |
D | ARG569 | electrostatic stabiliser |
D | ILE570 | electrostatic stabiliser |
D | ARG575 | electrostatic stabiliser |
D | GLY677 | electrostatic stabiliser |
D | PHE681 | covalently attached |