3DD1
Crystal structure of glycogen phophorylase complexed with an anthranilimide based inhibitor GSK254
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0002060 | molecular_function | purine nucleobase binding |
A | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
A | 0005515 | molecular_function | protein binding |
A | 0005524 | molecular_function | ATP binding |
A | 0005536 | molecular_function | D-glucose binding |
A | 0005576 | cellular_component | extracellular region |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0005975 | biological_process | carbohydrate metabolic process |
A | 0005977 | biological_process | glycogen metabolic process |
A | 0005980 | biological_process | glycogen catabolic process |
A | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
A | 0008184 | molecular_function | glycogen phosphorylase activity |
A | 0009617 | biological_process | response to bacterium |
A | 0016208 | molecular_function | AMP binding |
A | 0016757 | molecular_function | glycosyltransferase activity |
A | 0019842 | molecular_function | vitamin binding |
A | 0030170 | molecular_function | pyridoxal phosphate binding |
A | 0030246 | molecular_function | carbohydrate binding |
A | 0032052 | molecular_function | bile acid binding |
A | 0034774 | cellular_component | secretory granule lumen |
A | 0042593 | biological_process | glucose homeostasis |
A | 0042802 | molecular_function | identical protein binding |
A | 0070062 | cellular_component | extracellular exosome |
A | 0070266 | biological_process | necroptotic process |
A | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
A | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
A | 1904813 | cellular_component | ficolin-1-rich granule lumen |
B | 0000166 | molecular_function | nucleotide binding |
B | 0002060 | molecular_function | purine nucleobase binding |
B | 0004645 | molecular_function | 1,4-alpha-oligoglucan phosphorylase activity |
B | 0005515 | molecular_function | protein binding |
B | 0005524 | molecular_function | ATP binding |
B | 0005536 | molecular_function | D-glucose binding |
B | 0005576 | cellular_component | extracellular region |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0005975 | biological_process | carbohydrate metabolic process |
B | 0005977 | biological_process | glycogen metabolic process |
B | 0005980 | biological_process | glycogen catabolic process |
B | 0006015 | biological_process | 5-phosphoribose 1-diphosphate biosynthetic process |
B | 0008184 | molecular_function | glycogen phosphorylase activity |
B | 0009617 | biological_process | response to bacterium |
B | 0016208 | molecular_function | AMP binding |
B | 0016757 | molecular_function | glycosyltransferase activity |
B | 0019842 | molecular_function | vitamin binding |
B | 0030170 | molecular_function | pyridoxal phosphate binding |
B | 0030246 | molecular_function | carbohydrate binding |
B | 0032052 | molecular_function | bile acid binding |
B | 0034774 | cellular_component | secretory granule lumen |
B | 0042593 | biological_process | glucose homeostasis |
B | 0042802 | molecular_function | identical protein binding |
B | 0070062 | cellular_component | extracellular exosome |
B | 0070266 | biological_process | necroptotic process |
B | 0102250 | molecular_function | linear malto-oligosaccharide phosphorylase activity |
B | 0102499 | molecular_function | SHG alpha-glucan phosphorylase activity |
B | 1904813 | cellular_component | ficolin-1-rich granule lumen |
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 | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10949035, ECO:0007744|PDB:1FA9 |
Chain | Residue | Details |
A | ASP42 | |
A | TYR75 | |
A | ARG309 | |
B | ASP42 | |
B | TYR75 | |
B | ARG309 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Involved in the association of subunits => ECO:0000250|UniProtKB:P00489 |
Chain | Residue | Details |
A | CYS108 | |
A | CYS142 | |
B | CYS108 | |
B | CYS142 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | SITE: May be involved in allosteric control => ECO:0000250|UniProtKB:P00489 |
Chain | Residue | Details |
A | TYR155 | |
B | TYR155 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylalanine => ECO:0007744|PubMed:19413330 |
Chain | Residue | Details |
A | ALA1 | |
B | ALA1 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine; by PHK; in form phosphorylase a => ECO:0000269|PubMed:10949035, ECO:0000269|PubMed:22225877, ECO:0007744|PDB:1FA9 |
Chain | Residue | Details |
A | SEP14 | |
B | SEP14 |
site_id | SWS_FT_FI6 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9ET01 |
Chain | Residue | Details |
A | LYS363 | |
B | LYS363 |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:22225877 |
Chain | Residue | Details |
A | LYS469 | |
A | LYS795 | |
B | LYS469 | |
B | LYS795 |
site_id | SWS_FT_FI8 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9ET01 |
Chain | Residue | Details |
A | SER523 | |
B | SER523 |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P09811 |
Chain | Residue | Details |
A | SER560 | |
B | SER560 |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569 |
Chain | Residue | Details |
A | SER638 | |
B | SER638 |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10949035, ECO:0000269|PubMed:10980448, ECO:0000269|PubMed:12204691, ECO:0007744|PDB:1EM6, ECO:0007744|PDB:1EXV, ECO:0007744|PDB:1FA9, ECO:0007744|PDB:1FC0, ECO:0007744|PDB:1L5Q, ECO:0007744|PDB:1L5R, ECO:0007744|PDB:1L5S, ECO:0007744|PDB:1L7X |
Chain | Residue | Details |
A | LYS680 | |
B | 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 | CSA2 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1gpa |
Chain | Residue | Details |
B | ARG569 | |
B | LYS568 | |
B | THR676 | |
B | LYS574 |