1ABB
CONTROL OF PHOSPHORYLASE B CONFORMATION BY A MODIFIED COFACTOR: CRYSTALLOGRAPHIC STUDIES ON R-STATE GLYCOGEN PHOSPHORYLASE RECONSTITUTED WITH PYRIDOXAL 5'-DIPHOSPHATE
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 |
| 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 | obsolete linear malto-oligosaccharide phosphorylase activity |
| B | 0102499 | molecular_function | obsolete 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 | obsolete linear malto-oligosaccharide phosphorylase activity |
| C | 0102499 | molecular_function | obsolete 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 | obsolete linear malto-oligosaccharide phosphorylase activity |
| D | 0102499 | molecular_function | obsolete SHG alpha-glucan phosphorylase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 900 |
| Chain | Residue |
| A | LYS11 |
| A | SER14 |
| A | ARG16 |
| A | ARG69 |
| B | ARG43 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 900 |
| Chain | Residue |
| B | ARG69 |
| A | ARG43 |
| B | LYS11 |
| B | SER14 |
| B | ARG16 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 900 |
| Chain | Residue |
| C | LYS11 |
| C | SER14 |
| C | ARG16 |
| C | ARG69 |
| D | ARG43 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 D 900 |
| Chain | Residue |
| C | ARG43 |
| D | LYS11 |
| D | SER14 |
| D | ARG16 |
| D | ARG69 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PDP A 931 |
| Chain | Residue |
| A | ARG138 |
| A | TRP491 |
| A | LYS568 |
| A | ARG569 |
| A | LYS574 |
| A | ARG649 |
| A | VAL650 |
| A | THR676 |
| A | GLY677 |
| A | LYS680 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IMP A 920 |
| Chain | Residue |
| A | TRP67 |
| A | GLN71 |
| A | TYR75 |
| A | ARG309 |
| A | ARG310 |
| A | LYS315 |
| B | ASP42 |
| B | ASN44 |
| B | VAL45 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE PDP B 932 |
| Chain | Residue |
| B | TYR90 |
| B | ARG138 |
| B | TRP491 |
| B | LYS568 |
| B | ARG569 |
| B | LYS574 |
| B | ARG649 |
| B | VAL650 |
| B | ALA653 |
| B | THR676 |
| B | GLY677 |
| B | LYS680 |
| site_id | AC8 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE IMP B 920 |
| Chain | Residue |
| A | ASP42 |
| A | ASN44 |
| A | VAL45 |
| B | TRP67 |
| B | TYR75 |
| B | GLU76 |
| B | ARG309 |
| B | ARG310 |
| B | LYS315 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE PDP C 933 |
| Chain | Residue |
| C | TRP491 |
| C | LYS568 |
| C | ARG569 |
| C | LYS574 |
| C | TYR648 |
| C | ARG649 |
| C | VAL650 |
| C | ALA653 |
| C | THR676 |
| C | GLY677 |
| C | LYS680 |
| site_id | BC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE IMP C 920 |
| Chain | Residue |
| C | GLN71 |
| C | TYR75 |
| C | GLU76 |
| C | TYR155 |
| C | ARG309 |
| C | ARG310 |
| C | LYS315 |
| D | ASP42 |
| D | ASN44 |
| D | VAL45 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PDP D 934 |
| Chain | Residue |
| D | TYR90 |
| D | ARG138 |
| D | TRP491 |
| D | LYS568 |
| D | ARG569 |
| D | LYS574 |
| D | VAL650 |
| D | THR676 |
| D | GLY677 |
| D | LYS680 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE IMP D 920 |
| Chain | Residue |
| D | GLU76 |
| D | ARG309 |
| D | ARG310 |
| D | LYS315 |
| C | ASP42 |
| C | ASN44 |
| C | VAL45 |
| D | TRP67 |
| D | ILE68 |
| D | GLN71 |
| D | GLN72 |
| D | TYR75 |
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: 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_FI6 |
| 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_FI7 |
| 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_FI8 |
| 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_FI9 |
| 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_FI10 |
| 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 | 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 |
| site_id | CSA3 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gpa |
| Chain | Residue | Details |
| C | ARG569 | |
| C | LYS568 | |
| C | THR676 | |
| C | LYS574 |
| site_id | CSA4 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1gpa |
| 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 |
