5X0E

Free serine kinase (E30A mutant) in complex with phosphoserine and AMP

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

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d5x0ea_	Alpha and beta proteins (a+b)	ParB/Sulfiredoxin	ParB/Sulfiredoxin	Hypothetical protein PF0380	automated matches	(Thermococcus kodakarensis KOD1 ) [TaxId: 69014 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ParB/Sulfiredoxin	8087495	3001301	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	ParBc	e5x0eA1	A: a+b complex topology	X: ParB/Sulfiredoxin (From Topology)	H: ParB/Sulfiredoxin (From Topology)	T: ParB/Sulfiredoxin	F: ParBc	ECOD (1.6)
A	EUF08648	e5x0eA2	A: a/b three-layered sandwiches	X: Insert domain in hypothetical protein PF0380 (From Topology)	H: Insert domain in hypothetical protein PF0380 (From Topology)	T: Insert domain in hypothetical protein PF0380	F: EUF08648	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.1530.10	Alpha Beta	Alpha-Beta Complex	Conserved hypothetical protein from pyrococcus furiosus pfu- 392566-001, ParB domain	Conserved hypothetical protein from pyrococcus furiosus pfu- 392566-001, ParB domain	CATH (4.3.0)
A	3.30.1760.10	Alpha Beta	2-Layer Sandwich	Conserved hypothetical protein from pyrococcus furiosus pfu- 392566-001, domain 2	Conserved hypothetical protein from pyrococcus furiosus pfu- 392566-001, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF18231	Domain of unknown function (DUF5603) (DUF5603)	Domain of unknown function (DUF5603)	This domain is found in the C-terminal region of free serine kinase (SerK) in the hyperthermophilic archaeon Thermococcus kodakarensis. SerK converts ADP and l-serine (Ser) into AMP and O-phospho-l-serine (Sep), which is a precursor of l-cysteine. Th ...	This domain is found in the C-terminal region of free serine kinase (SerK) in the hyperthermophilic archaeon Thermococcus kodakarensis. SerK converts ADP and l-serine (Ser) into AMP and O-phospho-l-serine (Sep), which is a precursor of l-cysteine. The domain is not conserved in the ParB/Srx family. The differences between SerK and the other members of the ParB/Srx family is concentrated in the C-terminal region, which may include residues involved in the Sep binding [1].	Domain
A	PF02195	ParB/Sulfiredoxin domain (ParBc)	ParB/Sulfiredoxin domain	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Free serine 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 kinase activity transferase activity catalytic activity transferase activity, transferring phosphorus-containing groups	phosphorylation phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process serine family amino acid metabolic process oxoacid metabolic process sulfur amino acid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process cysteine biosynthetic process phosphorylation phosphate-containing compound metabolic process metabolic process cellular process phosphorus metabolic process serine family amino acid metabolic process oxoacid metabolic process sulfur amino acid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process cysteine biosynthetic process small molecule metabolic process sulfur compound metabolic process small molecule biosynthetic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-amino acid metabolic process cysteine metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process sulfur compound biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process serine family amino acid biosynthetic process sulfur amino acid biosynthetic process alpha-amino acid biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR040867	L-serine kinase SerK, C-terminal domain	Domain
A	IPR023098	L-serine kinase SerK/SbnI, C-terminal	Homologous Superfamily
A	IPR036086	ParB/Sulfiredoxin superfamily	Homologous Superfamily
A	IPR003115	ParB/Sulfiredoxin	Domain

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.