2PHK

THE CRYSTAL STRUCTURE OF A PHOSPHORYLASE KINASE PEPTIDE SUBSTRATE COMPLEX: KINASE SUBSTRATE RECOGNITION

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d2phka_	Alpha and beta proteins (a+b)	Protein kinase-like (PK-like)	Protein kinase-like (PK-like)	Protein kinases, catalytic subunit	gamma-subunit of glycogen phosphorylase kinase (Phk)	rabbit (Oryctolagus cuniculus ) [TaxId: 9986 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Protein kinase-like (PK-like)	8036619	3000066	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Pkinase_Tyr	e2phkA1	A: a+b complex topology	X: Protein kinase/SAICAR synthase/ATP-grasp (From Homology)	H: Protein kinase/SAICAR synthase/ATP-grasp	T: Protein kinase	F: Pkinase_Tyr	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.200.20	Alpha Beta	2-Layer Sandwich	Phosphorylase Kinase	domain 1	CATH (4.3.0)
A	1.10.510.10	Mainly Alpha	Orthogonal Bundle	Transferase(Phosphotransferase)	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00069	Protein kinase domain (Pkinase)	Protein kinase domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	PHOSPHORYLASE KINASE	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding protein binding calmodulin binding protein serine/threonine kinase activity tau-protein kinase activity catalytic activity, acting on a protein kinase activity protein kinase activity transferase activity catalytic activity phosphotransferase activity, alcohol group as acceptor transferase activity, transferring phosphorus-containing groups protein serine kinase activity phosphorylase kinase activity calcium/calmodulin-dependent protein kinase activity	carbohydrate metabolic process energy derivation by oxidation of organic compounds glycogen metabolic process primary metabolic process generation of precursor metabolites and energy glucan metabolic process polysaccharide metabolic process metabolic process cellular process energy reserve metabolic process macromolecule metabolic process	intracellular anatomical structure skeletal muscle myofibril intracellular membraneless organelle intracellular organelle cellular anatomical structure organelle membraneless organelle contractile muscle fiber cytoplasm supramolecular fiber myofibril supramolecular polymer supramolecular complex protein kinase complex intracellular anatomical structure skeletal muscle myofibril intracellular membraneless organelle intracellular organelle cellular anatomical structure organelle membraneless organelle contractile muscle fiber cytoplasm supramolecular fiber myofibril supramolecular polymer supramolecular complex protein kinase complex transferase complex, transferring phosphorus-containing groups protein-containing complex catalytic complex phosphorylase kinase complex serine/threonine protein kinase complex transferase complex
B	MC-PEPTIDE	-	-	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR017441	Protein kinase, ATP binding site	Binding Site
A	IPR002291	Phosphorylase kinase, gamma catalytic subunit	Family
A	IPR011009	Protein kinase-like domain superfamily	Homologous Superfamily
A	IPR000719	Protein kinase domain	Domain
A	IPR008271	Serine/threonine-protein kinase, active site	Active Site

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	phosphorylase kinase M-CSA #35	Eukaryotic protein kinases catalyse the transfer of ATP-gamma phosphate to serine, threonine and tyrosine residues on specific target proteins. The family of protein kinases represents one of the largest protein superfamilies, and structures of active kinases show similar conformations in key regions involved in ATP and protein substrate recognition domains. Phosphorylase kinase, the first protein kinase to be discovered, catalyses the phosphorylation of a single serine residue, Ser14 of inactive phosphorylase B (GPb). Phosphorylation converts the protein to active glycogen phosphorylase A (GPa), which catalyses glycogen degredation.	Defined by 5 residues: ASP:A-136 [auth A-149]LYS:A-138 [auth A-151]ASN:A-141 [auth A-154]ASP:A-154 [auth A-167]THR:A-173 [auth A-186] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.7.1.38 (PDB Primary Data) Search M-CSA Motif + EC 2.7.1.38 EC: 2.7.11.1 (UniProt) Search M-CSA Motif + EC 2.7.11.1 EC: 2.7.11.26 (UniProt) Search M-CSA Motif + EC 2.7.11.26 EC: 2.7.11.19 (UniProt) Search M-CSA Motif + EC 2.7.11.19

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.