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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

2P6B

Crystal Structure of Human Calcineurin in Complex with PVIVIT Peptide

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0033192molecular_functioncalmodulin-dependent protein phosphatase activity
A0097720biological_processcalcineurin-mediated signaling
B0001569biological_processbranching involved in blood vessel morphogenesis
B0001837biological_processepithelial to mesenchymal transition
B0004721molecular_functionphosphoprotein phosphatase activity
B0004723molecular_functioncalcium-dependent protein serine/threonine phosphatase activity
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005516molecular_functioncalmodulin binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
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
B0016020cellular_componentmembrane
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
C0016787molecular_functionhydrolase activity
C0033192molecular_functioncalmodulin-dependent protein phosphatase activity
C0097720biological_processcalcineurin-mediated signaling
D0001569biological_processbranching involved in blood vessel morphogenesis
D0001837biological_processepithelial to mesenchymal transition
D0004721molecular_functionphosphoprotein phosphatase activity
D0004723molecular_functioncalcium-dependent protein serine/threonine phosphatase activity
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005516molecular_functioncalmodulin binding
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005886cellular_componentplasma membrane
D0005955cellular_componentcalcineurin complex
D0006606biological_processprotein import into nucleus
D0007507biological_processheart development
D0008287cellular_componentprotein serine/threonine phosphatase complex
D0008597molecular_functioncalcium-dependent protein serine/threonine phosphatase regulator activity
D0014044biological_processSchwann cell development
D0016020cellular_componentmembrane
D0019902molecular_functionphosphatase binding
D0019904molecular_functionprotein domain specific binding
D0022011biological_processmyelination in peripheral nervous system
D0033173biological_processcalcineurin-NFAT signaling cascade
D0034504biological_processprotein localization to nucleus
D0042383cellular_componentsarcolemma
D0045202cellular_componentsynapse
D0045944biological_processpositive regulation of transcription by RNA polymerase II
D0046872molecular_functionmetal ion binding
D0060487biological_processlung epithelial cell differentiation
D0070886biological_processpositive regulation of calcineurin-NFAT signaling cascade
D0098685cellular_componentSchaffer collateral - CA1 synapse
D0098686cellular_componenthippocampal mossy fiber to CA3 synapse
D0098688cellular_componentparallel fiber to Purkinje cell synapse
D0098693biological_processregulation of synaptic vesicle cycle
D0098794cellular_componentpostsynapse
D0098978cellular_componentglutamatergic synapse
D0099149biological_processregulation of postsynaptic neurotransmitter receptor internalization
D0099170biological_processpostsynaptic modulation of chemical synaptic transmission
D1905665biological_processpositive regulation of calcium ion import across plasma membrane
D1905949biological_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 509
ChainResidue
AASP118
AASN150
AHIS199
AHIS281
AFE510
APO4511
site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 510
ChainResidue
AZN509
APO4511
AHOH673
AASP90
AHIS92
AASP118
site_idAC3
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 511
ChainResidue
AHIS92
AASP118
AARG122
AASN150
AHIS151
AARG254
AHIS281
AZN509
AFE510
AHOH538
AHOH554
AHOH615
site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 501
ChainResidue
BASP30
BASP32
BSER34
BSER36
BGLU41
BGLU68
site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 502
ChainResidue
BASP62
BASP64
BASN66
BGLU68
BGLU73
BHOH530
site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 503
ChainResidue
BASP99
BASP101
BASP103
BTYR105
BGLU110
BHOH521
site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 504
ChainResidue
BASP140
BASP142
BASP144
BARG146
BGLU151
BHOH532
site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE ZN C 512
ChainResidue
CASP118
CASN150
CHIS199
CHIS281
CFE513
CPO4514
site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE C 513
ChainResidue
CASP90
CHIS92
CASP118
CZN512
CPO4514
CHOH603
site_idBC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PO4 C 514
ChainResidue
CHIS92
CASP118
CARG122
CASN150
CHIS151
CARG254
CHIS281
CZN512
CFE513
CHOH611
CHOH623
site_idBC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 505
ChainResidue
DASP30
DASP32
DSER34
DSER36
DGLU41
DHOH533
site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 506
ChainResidue
DASP62
DASP64
DASN66
DGLU68
DGLU73
DHOH528
site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 507
ChainResidue
DASP99
DASP101
DASP103
DTYR105
DGLU110
DHOH523
site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 508
ChainResidue
DASP140
DASP142
DASP144
DARG146
DGLU151
DHOH530
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 Residues568
DetailsRegion: {"description":"Catalytic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues18
DetailsRegion: {"description":"Interaction with PxIxIF motif in substrate","evidences":[{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17502104","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues56
DetailsRegion: {"description":"Calcineurin B 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":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues8
DetailsMotif: {"description":"SAPNY motif","evidences":[{"source":"PubMed","id":"26248042","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"8524402","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12218175","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17498738","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22343722","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26248042","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":"1AUI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1M63","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2P6B","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3LL8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5C1V","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5SVE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6NUU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6UUQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues2
DetailsSite: {"description":"Interaction with PxVP motif in substrate","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27974827","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P63328","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues56
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues70
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues10
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_FI13
Number of Residues30
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_FI14
Number of Residues10
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_FI15
Number of Residues4
DetailsSite: {"description":"Interaction with PxVP motif in substrates of the catalytic subunit","evidences":[{"source":"PubMed","id":"23468591","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q63810","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues35
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
AASP121
AHIS151
site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
CASP121
CHIS151
site_idMCSA1
Number of Residues10
DetailsM-CSA 406
ChainResidueDetails
BILE106metal ligand
BASN108metal ligand
BLYS134metal ligand
BILE137electrostatic stabiliser
BASN138transition state stabiliser
BVAL166metal ligand
BVAL167proton shuttle (general acid/base)
site_idMCSA2
Number of Residues10
DetailsM-CSA 406
ChainResidueDetails
DILE106metal ligand
DASN108metal ligand
DLYS134metal ligand
DILE137electrostatic stabiliser
DASN138transition state stabiliser
DVAL166metal ligand
DVAL167proton shuttle (general acid/base)

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PDB entries from 2025-07-16

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