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 | 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 | 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 |
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 | 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 |
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 | 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 |
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 | 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 |
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 | 40 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"3616621","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | Site: {"description":"Involved in the association of subunits","evidences":[{"source":"PubMed","id":"728424","evidenceCode":"ECO:0000303"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Site: {"description":"Can be labeled by an AMP analog; may be involved in allosteric regulation","evidences":[{"source":"PubMed","id":"728424","evidenceCode":"ECO:0000303"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine; by PHK; in form phosphorylase A","evidences":[{"source":"UniProtKB","id":"P11217","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI7 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 4 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q9WUB3","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 12 |
Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09812","evidenceCode":"ECO:0000250"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 4 |
Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"7500360","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8976550","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2PRI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2SKE","evidenceCode":"ECO:0007744"}]} |
Chain | Residue | Details |
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 | HIS377 | electrostatic stabiliser |
A | LYS568 | electrostatic stabiliser |
A | ARG569 | electrostatic stabiliser |
A | LYS574 | electrostatic stabiliser |
A | THR676 | electrostatic stabiliser |
A | LYS680 | 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 | LYS680 | 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 | LYS680 | 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 | LYS680 | covalently attached |