1BG0

TRANSITION STATE STRUCTURE OF ARGININE KINASE

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	d1bg0a1	All alpha proteins	Guanido kinase N-terminal domain	Guanido kinase N-terminal domain	Guanido kinase N-terminal domain	Arginine kinase, N-domain	Atlantic horseshoe crab (Limulus polyphemus ) [TaxId: 6850 ],	SCOPe (2.08)
A	d1bg0a2	Alpha and beta proteins (a+b)	Glutamine synthetase/guanido kinase	Glutamine synthetase/guanido kinase	Guanido kinase catalytic domain	Arginine kinase, C-terminal domain	Atlantic horseshoe crab (Limulus polyphemus ) [TaxId: 6850 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Glutamine synthetase/guanido kinase	8038924	3000676	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Guanido kinase N-terminal domain	8038923	3000726	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	ATP-gua_PtransN	e1bg0A1	A: alpha arrays	X: Guanido kinase-N (From Topology)	H: Guanido kinase-N (From Topology)	T: Guanido kinase-N	F: ATP-gua_PtransN	ECOD (1.6)
A	ATP-gua_Ptrans	e1bg0A2	A: a+b two layers	X: Glutamine synthetase-like	H: Glutamine synthetase/guanido kinase (From Topology)	T: Glutamine synthetase/guanido kinase	F: ATP-gua_Ptrans	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.135.10	Mainly Alpha	Orthogonal Bundle	Transferase Creatine Kinase	Chain A, domain 1	CATH (4.3.0)
A	3.30.590.10	Alpha Beta	2-Layer Sandwich	Creatine Kinase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00217	ATP:guanido phosphotransferase, C-terminal catalytic domain (ATP-gua_Ptrans)	ATP:guanido phosphotransferase, C-terminal catalytic domain	The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain.	Domain
A	PF02807	ATP:guanido phosphotransferase, N-terminal domain (ATP-gua_PtransN)	ATP:guanido phosphotransferase, N-terminal domain	The N-terminal domain has an all-alpha fold.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ARGININE 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 creatine kinase activity kinase activity transferase activity catalytic activity phosphotransferase activity, nitrogenous group as acceptor transferase activity, transferring phosphorus-containing groups amino acid kinase activity arginine kinase activity	phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process phosphocreatine metabolic process phosphagen metabolic process phosphocreatine biosynthetic process cellular modified amino acid metabolic process phosphagen biosynthetic process biosynthetic process organophosphate metabolic process cellular modified amino acid biosynthetic process phosphorylation cellular metabolic process phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process phosphocreatine metabolic process phosphagen metabolic process phosphocreatine biosynthetic process cellular modified amino acid metabolic process phosphagen biosynthetic process biosynthetic process organophosphate metabolic process cellular modified amino acid biosynthetic process organophosphate biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR022415	ATP:guanido phosphotransferase active site	Active Site
A	IPR022413	ATP:guanido phosphotransferase, N-terminal	Domain
A	IPR022414	ATP:guanido phosphotransferase, catalytic domain	Domain
A	IPR036802	ATP:guanido phosphotransferase, N-terminal domain superfamily	Homologous Superfamily
A	IPR014746	Glutamine synthetase/guanido kinase, catalytic domain	Homologous Superfamily
A	IPR000749	ATP:guanido phosphotransferase	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	arginine kinase M-CSA #86	Arginine kinase and creatine kinase are members of the family of enzymes that catalyse the buffering of ATP in cells with fluctuating metabolic requirements.	Defined by 8 residues: ARG:A-125 [auth A-126]GLU:A-224 [auth A-225]ARG:A-228 [auth A-229]CYS:A-270 [auth A-271]THR:A-272 [auth A-273]ARG:A-279 [auth A-280]ARG:A-308 [auth A-309]GLU:A-313 [auth A-314] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.7.3.3 (PDB Primary Data) Search M-CSA Motif + EC 2.7.3.3

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.