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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9CHX

cryo-EM structure of calcineurin-fused beta2 adrenergic receptor in carazolol bound inactive state

Functional Information from GO Data
ChainGOidnamespacecontents
A0001569biological_processbranching involved in blood vessel morphogenesis
A0001837biological_processepithelial to mesenchymal transition
A0004721molecular_functionphosphoprotein phosphatase activity
A0004723molecular_functioncalcium-dependent protein serine/threonine phosphatase activity
A0004930molecular_functionG protein-coupled receptor activity
A0004935molecular_functionadrenergic receptor activity
A0004941molecular_functionbeta2-adrenergic receptor activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005955cellular_componentcalcineurin complex
A0006606biological_processprotein import into nucleus
A0006940biological_processregulation of smooth muscle contraction
A0007186biological_processG protein-coupled receptor signaling pathway
A0007189biological_processadenylate cyclase-activating G protein-coupled receptor signaling pathway
A0007507biological_processheart development
A0008287cellular_componentprotein serine/threonine phosphatase complex
A0008597molecular_functioncalcium-dependent protein serine/threonine phosphatase regulator activity
A0014044biological_processSchwann cell development
A0016020cellular_componentmembrane
A0019902molecular_functionphosphatase binding
A0019904molecular_functionprotein domain specific binding
A0022011biological_processmyelination in peripheral nervous system
A0033173biological_processcalcineurin-NFAT signaling cascade
A0034504biological_processprotein localization to nucleus
A0042383cellular_componentsarcolemma
A0045202cellular_componentsynapse
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0060487biological_processlung epithelial cell differentiation
A0070886biological_processpositive regulation of calcineurin-NFAT signaling cascade
A0097746biological_processblood vessel diameter maintenance
A0098685cellular_componentSchaffer collateral - CA1 synapse
A0098686cellular_componenthippocampal mossy fiber to CA3 synapse
A0098688cellular_componentparallel fiber to Purkinje cell synapse
A0098693biological_processregulation of synaptic vesicle cycle
A0098794cellular_componentpostsynapse
A0098978cellular_componentglutamatergic synapse
A0099149biological_processregulation of postsynaptic neurotransmitter receptor internalization
A0099170biological_processpostsynaptic modulation of chemical synaptic transmission
A1905665biological_processpositive regulation of calcium ion import across plasma membrane
A1905949biological_processnegative regulation of calcium ion import across plasma membrane
B0016787molecular_functionhydrolase activity
B0033192molecular_functioncalmodulin-dependent protein phosphatase activity
B0097720biological_processcalcineurin-mediated signaling
C0003007biological_processheart morphogenesis
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005160molecular_functiontransforming growth factor beta receptor binding
C0005246molecular_functioncalcium channel regulator activity
C0005515molecular_functionprotein binding
C0005527molecular_functionmacrolide binding
C0005528molecular_functionFK506 binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006457biological_processprotein folding
C0006458biological_process'de novo' protein folding
C0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
C0014802cellular_componentterminal cisterna
C0014809biological_processregulation of skeletal muscle contraction by regulation of release of sequestered calcium ion
C0016020cellular_componentmembrane
C0016529cellular_componentsarcoplasmic reticulum
C0016853molecular_functionisomerase activity
C0030018cellular_componentZ disc
C0030512biological_processnegative regulation of transforming growth factor beta receptor signaling pathway
C0030547molecular_functionsignaling receptor inhibitor activity
C0032880biological_processregulation of protein localization
C0032926biological_processnegative regulation of activin receptor signaling pathway
C0033017cellular_componentsarcoplasmic reticulum membrane
C0034713molecular_functiontype I transforming growth factor beta receptor binding
C0042026biological_processprotein refolding
C0042110biological_processT cell activation
C0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
C0044325molecular_functiontransmembrane transporter binding
C0050776biological_processregulation of immune response
C0051604biological_processprotein maturation
C0055010biological_processventricular cardiac muscle tissue morphogenesis
C0060347biological_processheart trabecula formation
C0070411molecular_functionI-SMAD binding
C0070697molecular_functionactivin receptor binding
C0097435biological_processsupramolecular fiber organization
C0098562cellular_componentcytoplasmic side of membrane
C1902991biological_processregulation of amyloid precursor protein catabolic process
C1990000biological_processamyloid fibril formation
C1990425cellular_componentryanodine receptor complex
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DLDNSGSLSveEF
ChainResidueDetails
AASP246-PHE258
AASP278-PHE290
AASP315-LEU327
AASP356-PHE368
site_idPS00125
Number of Residues6
DetailsSER_THR_PHOSPHATASE Serine/threonine specific protein phosphatases signature. LRGNHE
ChainResidueDetails
BLEU146-GLU151
site_idPS00237
Number of Residues17
DetailsG_PROTEIN_RECEP_F1_1 G-protein coupled receptors family 1 signature. ASIeTLCVIAVDRYFaI
ChainResidueDetails
AALA119-ILE135
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=1"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=2"}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues37
DetailsTopological domain: {"description":"Extracellular"}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=3"}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=4"}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=5"}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=6"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=7"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"18547522","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3D4S","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"17952055","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17962520","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2RH1","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"8521811","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17525332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues1
DetailsLipidation: {"description":"S-palmitoyl cysteine","evidences":[{"source":"PubMed","id":"27481942","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues28
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues35
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues5
DetailsRegion: {"description":"Calcineurin A binding","evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues15
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12357034","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31375679","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0000312"},{"source":"PDB","id":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1MF8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4F0Z","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4OR9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ORC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsSite: {"description":"Interaction with PxVP motif in substrates of the catalytic subunit","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q63810","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues9
DetailsRegion: {"description":"Interaction with PxIxIF motif in substrate","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues28
DetailsRegion: {"description":"Calcineurin B binding","evidences":[{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues4
DetailsMotif: {"description":"SAPNY motif","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"26794871","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"4ORB","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsSite: {"description":"Interaction with PxVP motif in substrate","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues1
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"PubMed","id":"16800626","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues88
DetailsDomain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26883","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idMCSA1
Number of Residues6
DetailsM-CSA 362
ChainResidueDetails
CTYR26electrostatic destabiliser, steric role
CPHE36electrostatic destabiliser, polar/non-polar interaction, steric role
CASP37electrostatic stabiliser, steric role
CILE56electrostatic stabiliser, steric role
CTYR82electrostatic stabiliser, steric role
CPHE99electrostatic destabiliser, polar/non-polar interaction, steric role

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PDB entries from 2025-07-23

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