Annotations: 1HJK

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1hjka_	Alpha and beta proteins (a/b)	Alkaline phosphatase-like	Alkaline phosphatase-like	Alkaline phosphatase	Alkaline phosphatase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1hjkb_	Alpha and beta proteins (a/b)	Alkaline phosphatase-like	Alkaline phosphatase-like	Alkaline phosphatase	Alkaline phosphatase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Alkaline phosphatase-like	8034139	3001353	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Alkaline phosphatase-like	8034139	3001353	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	Alk_phosphatase	e1hjkA1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: Alk_phosphatase	ECOD (1.6)
B	Alk_phosphatase	e1hjkB1	A: a/b three-layered sandwiches	X: Alkaline phosphatase-like (From Topology)	H: Alkaline phosphatase-like (From Topology)	T: Alkaline phosphatase-like	F: Alk_phosphatase	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.720.10	Alpha Beta	3-Layer(aba) Sandwich	Alkaline Phosphatase, subunit A	Alkaline Phosphatase, subunit A	CATH (4.3.0)
B	3.40.720.10	Alpha Beta	3-Layer(aba) Sandwich	Alkaline Phosphatase, subunit A	Alkaline Phosphatase, subunit A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00245	Alkaline phosphatase (Alk_phosphatase)	Alkaline phosphatase		Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	ALKALINE PHOSPHATASE	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity catalytic activity oxidoreductase activity, acting on phosphorus or arsenic in donors hydrogenase (acceptor) activity oxidoreductase activity, acting on hydrogen as donor transition metal ion binding zinc ion binding phosphoric ester hydrolase activity cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding oxidoreductase activity catalytic activity oxidoreductase activity, acting on phosphorus or arsenic in donors hydrogenase (acceptor) activity oxidoreductase activity, acting on hydrogen as donor transition metal ion binding zinc ion binding phosphoric ester hydrolase activity phosphoprotein phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds phosphatase activity hydrolase activity alkaline phosphatase activity	protein dephosphorylation dephosphorylation primary metabolic process macromolecule modification phosphate-containing compound metabolic process metabolic process cellular process protein metabolic process macromolecule metabolic process protein modification process phosphorus metabolic process	cellular anatomical structure periplasmic space outer membrane-bounded periplasmic space cell envelope

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR001952	Alkaline phosphatase	Family
A, B	IPR018299	Alkaline phosphatase, active site	Active Site
A, B	IPR017850	Alkaline-phosphatase-like, core domain superfamily	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B	SEP	Parent Component: SER RESID: AA0037 PSI-MOD : O-phospho-L-serine MOD:00046

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.