1FPZ

CRYSTAL STRUCTURE ANALYSIS OF KINASE ASSOCIATED PHOSPHATASE (KAP) WITH A SUBSTITUTION OF THE CATALYTIC SITE CYSTEINE (CYS140) TO A SERINE

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
Pharos: Disease Associations

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1fpza_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	Kinase associated phosphatase (kap)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
B	d1fpzb_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	Kinase associated phosphatase (kap)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
C	d1fpzc_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	Kinase associated phosphatase (kap)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
D	d1fpzd_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	Kinase associated phosphatase (kap)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
E	d1fpze_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	Kinase associated phosphatase (kap)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)
F	d1fpzf_	Alpha and beta proteins (a/b)	(Phosphotyrosine protein) phosphatases II	(Phosphotyrosine protein) phosphatases II	Dual specificity phosphatase-like	Kinase associated phosphatase (kap)	human (Homo sapiens ) [TaxId: 9606 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Dual specificity phosphatase-like	8020808	4000437	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	(Phosphotyrosine protein) phosphatases II	8033188	3000304	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8033188	3000304	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8033188	3000304	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8033188	3000304	SCOP2B (2022-06-29)
E	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8033188	3000304	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	(Phosphotyrosine protein) phosphatases II	8033188	3000304	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	PF05706	e1fpzA1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF05706	ECOD (1.6)
B	PF05706	e1fpzB1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF05706	ECOD (1.6)
C	PF05706	e1fpzC1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF05706	ECOD (1.6)
D	PF05706	e1fpzD1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF05706	ECOD (1.6)
E	PF05706	e1fpzE1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF05706	ECOD (1.6)
F	PF05706	e1fpzF1	A: a/b three-layered sandwiches	X: Flavodoxin-like	H: Flavoproteins/Phosphotyrosine protein phosphatases-like	T: (Phosphotyrosine protein) phosphatases II	F: PF05706	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
B	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
C	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
D	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
E	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)
F	3.90.190.10	Alpha Beta	Alpha-Beta Complex	Protein-Tyrosine Phosphatase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F	PF05706	Cyclin-dependent kinase inhibitor 3 (CDKN3) (CDKN3)	Cyclin-dependent kinase inhibitor 3 (CDKN3)	This family consists of cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphata ...	This family consists of cyclin-dependent kinase inhibitor 3 or kinase associated phosphatase proteins from several mammalian species. The cyclin-dependent kinase (Cdk)-associated protein phosphatase (KAP) is a human dual specificity protein phosphatase that dephosphorylates Cdk2 on threonine 160 in a cyclin-dependent manner [1,2].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F	CYCLIN-DEPENDENT KINASE INHIBITOR 3	phosphoric ester hydrolase activity phosphoprotein phosphatase activity protein serine/threonine phosphatase activity catalytic activity, acting on a protein hydrolase activity, acting on ester bonds myosin phosphatase activity phosphatase activity hydrolase activity catalytic activity protein tyrosine/serine/threonine phosphatase activity protein tyrosine phosphatase activity	negative regulation of cell population proliferation regulation of biological process cell population proliferation regulation of cellular process regulation of cell population proliferation negative regulation of cellular process biological regulation negative regulation of biological process cellular process mitotic cell cycle process cell cycle phase transition cell cycle G1/S transition of mitotic cell cycle cell cycle G1/S phase transition negative regulation of cell population proliferation regulation of biological process cell population proliferation regulation of cellular process regulation of cell population proliferation negative regulation of cellular process biological regulation negative regulation of biological process cellular process mitotic cell cycle process cell cycle phase transition cell cycle G1/S transition of mitotic cell cycle cell cycle G1/S phase transition mitotic cell cycle mitotic cell cycle phase transition cell cycle process regulation of cell cycle regulation of protein modification process regulation of catalytic activity regulation of protein phosphorylation regulation of cyclin-dependent protein kinase activity regulation of transferase activity regulation of primary metabolic process organic substance metabolic process regulation of cyclin-dependent protein serine/threonine kinase activity regulation of phosphate metabolic process phosphate-containing compound metabolic process protein metabolic process phosphorus metabolic process protein modification process organonitrogen compound metabolic process protein phosphorylation phosphorylation cellular metabolic process regulation of protein metabolic process regulation of cellular metabolic process primary metabolic process regulation of protein kinase activity regulation of macromolecule metabolic process regulation of molecular function regulation of kinase activity macromolecule modification regulation of protein serine/threonine kinase activity regulation of phosphorylation regulation of phosphorus metabolic process metabolic process macromolecule metabolic process regulation of metabolic process dephosphorylation	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol perinuclear region of cytoplasm membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F	IPR029021	Protein-tyrosine phosphatase-like	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F	IPR003595	Protein-tyrosine phosphatase, catalytic	Domain
A, B, C, D, E A, B, C, D, E, F	IPR000387	Tyrosine-specific protein phosphatases domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR020422	Dual specificity protein phosphatase domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR022778	CDKN3 domain	Domain
A, B, C, D, E A, B, C, D, E, F	IPR008425	Cyclin-dependent kinase inhibitor 3	Family

Pharos: Disease Associations Pharos Homepage Annotation

Chains	Drug Target	Associated Disease
A, B, C, D, E A, B, C, D, E, F	Pharos: Q16667	Liver Cirrhosis, Experimental hepatocellular carcinoma malignant ependymoma malignant pancreatic neoplasm oligodendroglioma pancreatic intraductal papillary-mucinous neoplasm acute myeloid leukemia ulcerative colitis atopic eczema breast carcinoma endometriosis interstitial cystitis liver cancer lung adenocarcinoma malignant glioma Liver Cirrhosis, Experimental hepatocellular carcinoma malignant ependymoma malignant pancreatic neoplasm oligodendroglioma pancreatic intraductal papillary-mucinous neoplasm acute myeloid leukemia ulcerative colitis atopic eczema breast carcinoma endometriosis interstitial cystitis liver cancer lung adenocarcinoma malignant glioma medulloblastoma ovarian cancer primitive neuroectodermal tumor adrenal cortex carcinoma atypical teratoid rhabdoid tumor cancer glioblastoma invasive ductal breast carcinoma lung cancer malignant mesothelioma non-small cell lung carcinoma pancreatic intraductal papillary-mucinous carcinoma psoriasis astrocytic tumor breast cancer ductal breast carcinoma in situ hepatoblastoma IgA glomerulonephritis large cell medulloblastoma

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.