Brand  (β version)

PDB ID: 1QL6

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Ligands
Code Name Style Show Link
ATP Adenosine-5'-triphosphate PoSSuM
MN Manganese (II) ion PoSSuM
SO4 Sulfate ion PoSSuM
Non-standard Residues
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Glycosylation
Code Name Emphasize
Modification
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Structure summary

Code : 1QL6   PDBj   RCSB PDB   PDBe
Header : KINASE (GLYCOGEN METABOLISM)
Title : THE CATALYTIC MECHANISM OF PHOSPHORYLASE KINASE PROBED BY MUTATIONAL STUDIES
Release Data : 1999-12-14
Compound :
mol_id molecule chains synonym
1 PHOSPHORYLASE KINASE A RABBIT MUSCLE PHOSPHORYLASE KINASE
ec: 2.7.1.38
fragment: GAMMA SUBUNIT, TRUNCATED TO RESIDUES 1 - 298
mutation: YES
other_details: LIGANDS ATP AND MN(II)
Source :
mol_id organism_scientific organism_common expression_system
1 ORYCTOLAGUS CUNICULUS  (taxid:9986) RABBIT ESCHERICHIA COLI  (taxid:562)
tissue: SKELETAL MUSCLE
expression_system_plasmid: PMW172
Authors : Skamnaki, V.T., Owen, D.J., Noble, M.E.M., Lowe, E.D., Oikonomakos, N.G., Johnson, L.N.
Keywords : KINASE (GLYCOGEN METABOLISM), GLYCOGEN METABOLISM, TRANSFERASE, SERINE/THREONINE-PROTEIN, KINASE, ATP-BINDING, CALMODULIN-BINDING
Exp. method : X-RAY DIFFRACTION ( 2.4 Å )
Citation :

Catalytic Mechanism of Phosphorylase Kinase Probed by Mutational Studies.

Skamnaki, V.T.,Owen, D.J.,Noble, M.E.  et al.
(1999)  Biochemistry  38 : 14718

PubMed: 10545198
DOI: 10.1021/BI991454F

The Crystal Structure of a Phosphorylase Kinase Peptide Substrate Complex: Kinase Substrate Recognition

Lowe, E.D.,Noble, M.E.M.,Skamnaki, V.T.  et al.
(1997)  Embo J.  16 : 6646

PubMed: 9362479
DOI: 10.1093/EMBOJ/16.22.6646

Reaction

Chain : A
UniProt : P00518 (PHKG1_RABIT)
Reaction: EC: Evidence:
Physiological Direction:
2 ATP + phosphorylase b = 2 ADP + phosphorylase a. 2.7.11.19 -
-
ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl- [tau protein] 2.7.11.26 -
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ATP + L-threonyl-[tau protein] = ADP + H(+) + O-phospho-L- threonyl-[tau protein] 2.7.11.26 -
-
ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl- [protein] 2.7.11.1 -
-
ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L- threonyl-[protein] 2.7.11.1 -
-