4KBP

KIDNEY BEAN PURPLE ACID PHOSPHATASE

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	d4kbpa1	All beta proteins	Immunoglobulin-like beta-sandwich	Purple acid phosphatase, N-terminal domain	Purple acid phosphatase, N-terminal domain	Purple acid phosphatase, N-terminal domain	(Phaseolus vulgaris ) [TaxId: 3885 ],	SCOPe (2.08)
A	d4kbpa2	Alpha and beta proteins (a+b)	Metallo-dependent phosphatases	Metallo-dependent phosphatases	Purple acid phosphatase-like	Plant purple acid phosphatase, catalytic domain	(Phaseolus vulgaris ) [TaxId: 3885 ],	SCOPe (2.08)
B	d4kbpb1	All beta proteins	Immunoglobulin-like beta-sandwich	Purple acid phosphatase, N-terminal domain	Purple acid phosphatase, N-terminal domain	Purple acid phosphatase, N-terminal domain	(Phaseolus vulgaris ) [TaxId: 3885 ],	SCOPe (2.08)
B	d4kbpb2	Alpha and beta proteins (a+b)	Metallo-dependent phosphatases	Metallo-dependent phosphatases	Purple acid phosphatase-like	Plant purple acid phosphatase, catalytic domain	(Phaseolus vulgaris ) [TaxId: 3885 ],	SCOPe (2.08)
C	d4kbpc1	All beta proteins	Immunoglobulin-like beta-sandwich	Purple acid phosphatase, N-terminal domain	Purple acid phosphatase, N-terminal domain	Purple acid phosphatase, N-terminal domain	(Phaseolus vulgaris ) [TaxId: 3885 ],	SCOPe (2.08)
C	d4kbpc2	Alpha and beta proteins (a+b)	Metallo-dependent phosphatases	Metallo-dependent phosphatases	Purple acid phosphatase-like	Plant purple acid phosphatase, catalytic domain	(Phaseolus vulgaris ) [TaxId: 3885 ],	SCOPe (2.08)
D	d4kbpd1	All beta proteins	Immunoglobulin-like beta-sandwich	Purple acid phosphatase, N-terminal domain	Purple acid phosphatase, N-terminal domain	Purple acid phosphatase, N-terminal domain	(Phaseolus vulgaris ) [TaxId: 3885 ],	SCOPe (2.08)
D	d4kbpd2	Alpha and beta proteins (a+b)	Metallo-dependent phosphatases	Metallo-dependent phosphatases	Purple acid phosphatase-like	Plant purple acid phosphatase, catalytic domain	(Phaseolus vulgaris ) [TaxId: 3885 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Purple acid phosphatase N-terminal domain-like	8055339	3002043	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Metallo-dependent phosphatases	8035923	3001067	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Purple acid phosphatase N-terminal domain-like	8055339	3002043	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Metallo-dependent phosphatases	8035923	3001067	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Metallo-dependent phosphatases	8035923	3001067	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Purple acid phosphatase N-terminal domain-like	8055339	3002043	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Metallo-dependent phosphatases	8035923	3001067	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Purple acid phosphatase N-terminal domain-like	8055339	3002043	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	Pur_ac_phosph_N	e4kbpA1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Pur_ac_phosph_N	ECOD (1.6)
A	PhoD_1	e4kbpA2	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Metallo-dependent phosphatases (From Topology)	T: Metallo-dependent phosphatases	F: PhoD_1	ECOD (1.6)
B	Pur_ac_phosph_N	e4kbpB1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Pur_ac_phosph_N	ECOD (1.6)
B	PhoD_1	e4kbpB2	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Metallo-dependent phosphatases (From Topology)	T: Metallo-dependent phosphatases	F: PhoD_1	ECOD (1.6)
C	Pur_ac_phosph_N	e4kbpC1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Pur_ac_phosph_N	ECOD (1.6)
C	PhoD_1	e4kbpC2	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Metallo-dependent phosphatases (From Topology)	T: Metallo-dependent phosphatases	F: PhoD_1	ECOD (1.6)
D	Pur_ac_phosph_N	e4kbpD1	A: beta sandwiches	X: Immunoglobulin-like beta-sandwich	H: Immunoglobulin-related	T: Immunoglobulin/Fibronectin type III/E set domains/PapD-like	F: Pur_ac_phosph_N	ECOD (1.6)
D	PhoD_1	e4kbpD2	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Metallo-dependent phosphatases (From Topology)	T: Metallo-dependent phosphatases	F: PhoD_1	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.60.40.380	Mainly Beta	Sandwich	Immunoglobulin-like	Purple acid phosphatase-like, N-terminal	CATH (4.3.0)
A	3.60.21.10	Alpha Beta	4-Layer Sandwich	Purple Acid Phosphatase	chain A, domain 2	CATH (4.3.0)
B	2.60.40.380	Mainly Beta	Sandwich	Immunoglobulin-like	Purple acid phosphatase-like, N-terminal	CATH (4.3.0)
B	3.60.21.10	Alpha Beta	4-Layer Sandwich	Purple Acid Phosphatase	chain A, domain 2	CATH (4.3.0)
C	2.60.40.380	Mainly Beta	Sandwich	Immunoglobulin-like	Purple acid phosphatase-like, N-terminal	CATH (4.3.0)
C	3.60.21.10	Alpha Beta	4-Layer Sandwich	Purple Acid Phosphatase	chain A, domain 2	CATH (4.3.0)
D	2.60.40.380	Mainly Beta	Sandwich	Immunoglobulin-like	Purple acid phosphatase-like, N-terminal	CATH (4.3.0)
D	3.60.21.10	Alpha Beta	4-Layer Sandwich	Purple Acid Phosphatase	chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00149	Calcineurin-like phosphoesterase (Metallophos)	Calcineurin-like phosphoesterase	This family includes a diverse range of phosphoesterases [1], including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD Swiss:P13457 or ...	This family includes a diverse range of phosphoesterases [1], including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD Swiss:P13457 or yeast MRE11 Swiss:P32829. The most conserved regions in this superfamily centre around the metal chelating residues.	Domain
A, B, C, D	PF16656	Purple acid Phosphatase, N-terminal domain (Pur_ac_phosph_N)	Purple acid Phosphatase, N-terminal domain	This domain is found at the N-terminus of Purple acid phosphatase proteins.	Domain
A, B, C, D	PF14008	Iron/zinc purple acid phosphatase-like protein C (Metallophos_C)	Iron/zinc purple acid phosphatase-like protein C	This domain is found at the C-terminus of Purple acid phosphatase proteins.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	PURPLE ACID PHOSPHATASE	cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding phosphoric ester hydrolase activity acid phosphatase activity hydrolase activity, acting on ester bonds phosphatase activity hydrolase activity catalytic activity ferric iron binding cation binding transition metal ion binding zinc ion binding ion binding binding metal ion binding small molecule binding phosphoric ester hydrolase activity acid phosphatase activity hydrolase activity, acting on ester bonds phosphatase activity hydrolase activity catalytic activity ferric iron binding iron ion binding	-	extracellular region cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR004843	Calcineurin-like phosphoesterase domain, ApaH type	Domain
A, B, C, D	IPR025733	Iron/zinc purple acid phosphatase-like C-terminal domain	Domain
A, B, C, D	IPR041792	Purple acid phosphatase, metallophosphatase domain	Domain
A, B, C, D	IPR008963	Purple acid phosphatase-like, N-terminal	Homologous Superfamily
A, B, C, D	IPR015914	Purple acid phosphatase, N-terminal	Domain
A, B, C, D	IPR029052	Metallo-dependent phosphatase-like	Homologous Superfamily
A, B, C, D	IPR039331	Purple acid phosphatase-like	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	purple acid phosphatase M-CSA #43	Purple acid phosphatases (PAPs) are metalloenzymes found in animals, plants and fungi. They possess a binuclear metal centre to catalyse the hydrolysis of phosphate esters (e.g. of sugars or proteins) and anhydrides (e.g. ATP) under acidic conditions. The distinctive purple colour of these enzymes is due to a metal to ligand charge transfer from a tyrosine phenolate to a chromophoric Fe(III). The cornerstone of the active site of PAP is the presence of two metal ions; Fe(III) is always present in the chromophoric site, while the second site can be occupied by a redox active Fe(II/III) in mammals or a Zn(II) or Mn(II) in plants. Crystal structures of human, pig, rat, and plant PAPs have been determined and show that the amino acid ligands of the metal ions are completely conserved across plant and animal PAPs, but there are some differences in the identities of the residues that line the active site.	Defined by 10 residues: ASP:A-135ASP:A-164TYR:A-167ASN:A-201HIS:A-202HIS:A-286HIS:A-295HIS:A-296HIS:A-323HIS:A-325 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.1.3.2 (PDB Primary Data) Search M-CSA Motif + EC 3.1.3.2

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.