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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

4ORB

Crystal structure of mouse calcineurin

Functional Information from GO Data
ChainGOidnamespacecontents
A0000082biological_processG1/S transition of mitotic cell cycle
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0004723molecular_functioncalcium-dependent protein serine/threonine phosphatase activity
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005955cellular_componentcalcineurin complex
A0006470biological_processprotein dephosphorylation
A0006606biological_processprotein import into nucleus
A0006816biological_processcalcium ion transport
A0008287cellular_componentprotein serine/threonine phosphatase complex
A0008544biological_processepidermis development
A0009898cellular_componentcytoplasmic side of plasma membrane
A0010613biological_processpositive regulation of cardiac muscle hypertrophy
A0010628biological_processpositive regulation of gene expression
A0010629biological_processnegative regulation of gene expression
A0014883biological_processtransition between fast and slow fiber
A0014898biological_processcardiac muscle hypertrophy in response to stress
A0016787molecular_functionhydrolase activity
A0019722biological_processcalcium-mediated signaling
A0019899molecular_functionenzyme binding
A0023057biological_processnegative regulation of signaling
A0030018cellular_componentZ disc
A0030216biological_processkeratinocyte differentiation
A0030335biological_processpositive regulation of cell migration
A0033173biological_processcalcineurin-NFAT signaling cascade
A0033192molecular_functioncalmodulin-dependent protein phosphatase activity
A0033555biological_processmulticellular organismal response to stress
A0036057cellular_componentslit diaphragm
A0042104biological_processpositive regulation of activated T cell proliferation
A0042383cellular_componentsarcolemma
A0043161biological_processproteasome-mediated ubiquitin-dependent protein catabolic process
A0043197cellular_componentdendritic spine
A0044877molecular_functionprotein-containing complex binding
A0045202cellular_componentsynapse
A0045669biological_processpositive regulation of osteoblast differentiation
A0045672biological_processpositive regulation of osteoclast differentiation
A0045785biological_processpositive regulation of cell adhesion
A0045807biological_processpositive regulation of endocytosis
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046676biological_processnegative regulation of insulin secretion
A0046872molecular_functionmetal ion binding
A0046878biological_processpositive regulation of saliva secretion
A0046983molecular_functionprotein dimerization activity
A0048741biological_processskeletal muscle fiber development
A0050774biological_processnegative regulation of dendrite morphogenesis
A0050804biological_processmodulation of chemical synaptic transmission
A0051117molecular_functionATPase binding
A0051592biological_processresponse to calcium ion
A0060079biological_processexcitatory postsynaptic potential
A0061006biological_processregulation of cell proliferation involved in kidney morphogenesis
A0070294biological_processrenal sodium ion absorption
A0070886biological_processpositive regulation of calcineurin-NFAT signaling cascade
A0071333biological_processcellular response to glucose stimulus
A0090193biological_processpositive regulation of glomerulus development
A0097205biological_processrenal filtration
A0097720biological_processcalcineurin-mediated signaling
A0098685cellular_componentSchaffer collateral - CA1 synapse
A0098978cellular_componentglutamatergic synapse
A0099170biological_processpostsynaptic modulation of chemical synaptic transmission
A0110062biological_processnegative regulation of angiotensin-activated signaling pathway
A0110063biological_processpositive regulation of angiotensin-activated signaling pathway
A1903235biological_processpositive regulation of calcium ion-dependent exocytosis of neurotransmitter
A1903244biological_processpositive regulation of cardiac muscle hypertrophy in response to stress
A1905205biological_processpositive regulation of connective tissue replacement
A1905665biological_processpositive regulation of calcium ion import across plasma membrane
A1905949biological_processnegative regulation of calcium ion import across plasma membrane
B0001569biological_processbranching involved in blood vessel morphogenesis
B0001837biological_processepithelial to mesenchymal transition
B0004721molecular_functionphosphoprotein phosphatase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005955cellular_componentcalcineurin complex
B0006606biological_processprotein import into nucleus
B0007507biological_processheart development
B0008287cellular_componentprotein serine/threonine phosphatase complex
B0008597molecular_functioncalcium-dependent protein serine/threonine phosphatase regulator activity
B0014044biological_processSchwann cell development
B0019902molecular_functionphosphatase binding
B0019904molecular_functionprotein domain specific binding
B0022011biological_processmyelination in peripheral nervous system
B0033173biological_processcalcineurin-NFAT signaling cascade
B0034504biological_processprotein localization to nucleus
B0042383cellular_componentsarcolemma
B0045202cellular_componentsynapse
B0045944biological_processpositive regulation of transcription by RNA polymerase II
B0046872molecular_functionmetal ion binding
B0060487biological_processlung epithelial cell differentiation
B0070886biological_processpositive regulation of calcineurin-NFAT signaling cascade
B0098685cellular_componentSchaffer collateral - CA1 synapse
B0098686cellular_componenthippocampal mossy fiber to CA3 synapse
B0098688cellular_componentparallel fiber to Purkinje cell synapse
B0098693biological_processregulation of synaptic vesicle cycle
B0098794cellular_componentpostsynapse
B0098978cellular_componentglutamatergic synapse
B0099149biological_processregulation of postsynaptic neurotransmitter receptor internalization
B0099170biological_processpostsynaptic modulation of chemical synaptic transmission
B1905665biological_processpositive regulation of calcium ion import across plasma membrane
B1905949biological_processnegative regulation of calcium ion import across plasma membrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
AASP90
AASP118
AASN150
AHIS199
AHIS281
AFE602
site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 602
ChainResidue
AZN601
AHOH712
AASP90
AHIS92
AASP118
site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 201
ChainResidue
BASP62
BASP64
BASN66
BGLU68
BGLU73
BHOH301
site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 202
ChainResidue
BASP99
BASP101
BASP103
BTYR105
BGLU110
BHOH302
site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 203
ChainResidue
BASP140
BASP142
BASP144
BARG146
BGLU151
BHOH303
site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 204
ChainResidue
BASP30
BASP32
BSER34
BSER36
BGLU41
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF
ChainResidueDetails
BASP30-PHE42
BASP62-PHE74
BASP99-LEU111
BASP140-PHE152
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
ALEU147-GLU152
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues284
DetailsRegion: {"description":"Catalytic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues9
DetailsRegion: {"description":"Interaction with PxIxIF motif in substrate","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues28
DetailsRegion: {"description":"Calcineurin B binding","evidences":[{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues4
DetailsMotif: {"description":"SAPNY motif","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ORB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Interaction with PxVP motif in substrate","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"PubMed","id":"16800626","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P63329","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues28
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues35
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues5
DetailsRegion: {"description":"Calcineurin A binding","evidences":[{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ORB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsSite: {"description":"Interaction with PxVP motif in substrates of the catalytic subunit","evidences":[{"source":"UniProtKB","id":"P63098","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18034455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

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PDB entries from 2025-10-29

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