6TZ6

Crystal Structure of Candida Albicans Calcineurin A, Calcineurin B, FKBP12 and FK506 (Tacrolimus)

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)
B	d6tz6b_	All alpha proteins	EF Hand-like	EF-hand	automated matches	automated matches	Yeast (Candida albicans WO-1 ) [TaxId: 294748 ],	SCOPe (2.08)
E	d6tz6e_	All alpha proteins	EF Hand-like	EF-hand	automated matches	automated matches	Yeast (Candida albicans WO-1 ) [TaxId: 294748 ],	SCOPe (2.08)
C	d6tz6c_	Alpha and beta proteins (a+b)	FKBP-like	FKBP-like	automated matches	automated matches	Yeast (Candida albicans SC5314 ) [TaxId: 237561 ],	SCOPe (2.08)
F	d6tz6f_	Alpha and beta proteins (a+b)	FKBP-like	FKBP-like	automated matches	automated matches	Yeast (Candida albicans SC5314 ) [TaxId: 237561 ],	SCOPe (2.08)
A	d6tz6a_	Alpha and beta proteins (a+b)	Metallo-dependent phosphatases	Metallo-dependent phosphatases	Protein serine/threonine phosphatase	automated matches	Yeast (Candida albicans WO-1 ) [TaxId: 294748 ],	SCOPe (2.08)
D	d6tz6d_	Alpha and beta proteins (a+b)	Metallo-dependent phosphatases	Metallo-dependent phosphatases	Protein serine/threonine phosphatase	automated matches	Yeast (Candida albicans WO-1 ) [TaxId: 294748 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	EF-hand	8097428	3001983	SCOP2B (2022-06-29)
E	SCOP2 Family	Calmodulin-like	8097427	4000924	SCOP2 (2022-06-29)
E	SCOP2 Superfamily	EF-hand	8097428	3001983	SCOP2 (2022-06-29)
C	SCOP2B Superfamily	Rotamase-like	8065270	3000622	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Rotamase-like	8065270	3000622	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)
B	PF00036	e6tz6B1	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF00036	ECOD (1.6)
B	PF13499	e6tz6B2	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF13499	ECOD (1.6)
E	PF00036	e6tz6E1	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF00036	ECOD (1.6)
E	PF13499	e6tz6E2	A: alpha arrays	X: EF-hand	H: EF-hand-related	T: EF-hand	F: PF13499	ECOD (1.6)
C	PF00254	e6tz6C1	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF00254	ECOD (1.6)
F	PF00254	e6tz6F1	A: a+b two layers	X: FKBP-like	H: FKBP-like	T: FKBP-like	F: PF00254	ECOD (1.6)
A	PF00149	e6tz6A1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Metallo-dependent phosphatases (From Topology)	T: Metallo-dependent phosphatases	F: PF00149	ECOD (1.6)
D	PF00149	e6tz6D1	A: a+b four layers	X: Carbon-nitrogen hydrolase-like	H: Metallo-dependent phosphatases (From Topology)	T: Metallo-dependent phosphatases	F: PF00149	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	1.10.238.10	Mainly Alpha	Orthogonal Bundle	Recoverin	domain 1	CATH (utative)
E	1.10.238.10	Mainly Alpha	Orthogonal Bundle	Recoverin	domain 1	CATH (utative)
C	3.10.50.40	Alpha Beta	Roll	Chitinase A	domain 3	CATH (utative)
F	3.10.50.40	Alpha Beta	Roll	Chitinase A	domain 3	CATH (utative)
A	3.60.21.10	Alpha Beta	4-Layer Sandwich	Purple Acid Phosphatase	chain A, domain 2	CATH (utative)
D	3.60.21.10	Alpha Beta	4-Layer Sandwich	Purple Acid Phosphatase	chain A, domain 2	CATH (utative)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
B, E	PF13499	EF-hand domain pair (EF-hand_7)	EF-hand domain pair	-	Domain
C, F	PF00254	FKBP-type peptidyl-prolyl cis-trans isomerase (FKBP_C)	FKBP-type peptidyl-prolyl cis-trans isomerase	-	Domain
A, 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

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
B, E	Calcineurin subunit B	cation binding ion binding binding calcium ion binding metal ion binding small molecule binding enzyme regulator activity calcium-dependent protein serine/threonine phosphatase regulator activity phosphatase regulator activity molecular function regulator activity protein phosphatase regulator activity	-	-
C, F	FK506-binding protein 1	isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity binding organic cyclic compound binding macrolide binding	organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process protein folding biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process organonitrogen compound metabolic process cellular biosynthetic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process protein maturation organic substance metabolic process protein folding biosynthetic process organic substance biosynthetic process metabolic process cellular process protein metabolic process macromolecule metabolic process regulation of cellular process serine family amino acid metabolic process oxoacid metabolic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process alpha-amino acid metabolic process carboxylic acid biosynthetic process regulation of primary metabolic process homoserine biosynthetic process cellular ketone metabolic process regulation of small molecule metabolic process small molecule metabolic process regulation of homoserine biosynthetic process regulation of biosynthetic process regulation of biological process regulation of cellular ketone metabolic process regulation of cellular amino acid metabolic process small molecule biosynthetic process regulation of amine metabolic process biological regulation carboxylic acid metabolic process regulation of cellular metabolic process L-amino acid biosynthetic process regulation of cellular amino acid biosynthetic process L-amino acid metabolic process regulation of cellular biosynthetic process amine metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process proteinogenic amino acid biosynthetic process homoserine metabolic process serine family amino acid biosynthetic process regulation of metabolic process alpha-amino acid biosynthetic process protein-DNA complex organization cellular component organization protein-containing complex organization chromatin organization cellular component organization or biogenesis	cell periphery extracellular matrix biofilm matrix external encapsulating structure fungal biofilm matrix cellular anatomical entity intracellular anatomical structure cytoplasm extracellular region
A, D	Serine/threonine-protein phosphatase	protein binding binding calmodulin binding 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 cation binding ion binding protein binding binding calmodulin binding 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 cation binding ion binding metal ion binding small molecule binding calmodulin-dependent protein phosphatase activity calcium-dependent protein serine/threonine phosphatase activity	cellular response to stimulus regulation of biological process regulation of cellular process response to stimulus signaling biological regulation intracellular signal transduction cell communication calcium-mediated signaling intracellular signaling cassette cellular process signal transduction calcineurin-mediated signaling	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
B, E	IPR018247	EF-Hand 1, calcium-binding site	Binding Site
B, E	IPR015757	Calcineurin B protein	Family
B, E	IPR002048	EF-hand domain	Domain
B, E	IPR011992	EF-hand domain pair	Homologous Superfamily
C, F	IPR046357	Peptidyl-prolyl cis-trans isomerase domain superfamily	Homologous Superfamily
C, F	IPR001179	FKBP-type peptidyl-prolyl cis-trans isomerase domain	Domain
A, D	IPR004843	Calcineurin-like phosphoesterase domain, ApaH type	Domain
A, D	IPR006186	Serine/threonine-specific protein phosphatase/bis(5-nucleosyl)-tetraphosphatase	Domain
A, D	IPR043360	PP2B	Family
A, D	IPR041751	PP2B, metallophosphatase domain	Domain
A, D	IPR029052	Metallo-dependent phosphatase-like	Homologous Superfamily

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 R01GM133198.