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1MF8

Crystal Structure of human calcineurin complexed with cyclosporin A and human cyclophilin

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
C0000413biological_processprotein peptidyl-prolyl isomerization
C0001933biological_processnegative regulation of protein phosphorylation
C0001934biological_processpositive regulation of protein phosphorylation
C0003723molecular_functionRNA binding
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005178molecular_functionintegrin binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005925cellular_componentfocal adhesion
C0006457biological_processprotein folding
C0006469biological_processnegative regulation of protein kinase activity
C0006915biological_processapoptotic process
C0016018molecular_functioncyclosporin A binding
C0016020cellular_componentmembrane
C0016853molecular_functionisomerase activity
C0019076biological_processviral release from host cell
C0030168biological_processplatelet activation
C0030182biological_processneuron differentiation
C0030593biological_processneutrophil chemotaxis
C0030595biological_processleukocyte chemotaxis
C0031982cellular_componentvesicle
C0032148biological_processactivation of protein kinase B activity
C0032873biological_processnegative regulation of stress-activated MAPK cascade
C0032991cellular_componentprotein-containing complex
C0034389biological_processlipid droplet organization
C0034599biological_processcellular response to oxidative stress
C0034774cellular_componentsecretory granule lumen
C0042118biological_processendothelial cell activation
C0043410biological_processpositive regulation of MAPK cascade
C0045069biological_processregulation of viral genome replication
C0045070biological_processpositive regulation of viral genome replication
C0046790molecular_functionvirion binding
C0050714biological_processpositive regulation of protein secretion
C0051082molecular_functionunfolded protein binding
C0051092biological_processpositive regulation of NF-kappaB transcription factor activity
C0060352biological_processcell adhesion molecule production
C0061944biological_processnegative regulation of protein K48-linked ubiquitination
C0070062cellular_componentextracellular exosome
C0070527biological_processplatelet aggregation
C1902176biological_processnegative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway
C1903901biological_processnegative regulation of viral life cycle
C1904399molecular_functionheparan sulfate binding
C1904813cellular_componentficolin-1-rich granule lumen
C2001233biological_processregulation of apoptotic signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASP30
BASP32
BSER34
BSER36
BGLU41

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 402
ChainResidue
BGLU73
BASP62
BASP64
BASN66
BGLU68

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
BASP99
BASP101
BASP103
BTYR105
BGLU110

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 404
ChainResidue
BASP140
BASP142
BASP144
BARG146
BGLU151

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE PO4 A 393
ChainResidue
AARG122
ATYR311

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR CHAIN D OF CYCLOSPORIN A
ChainResidue
ALEU312
AVAL314
ATYR341
ATRP342
ALEU343
APRO344
ATRP352
APHE356
BASN122
CARG55
CPHE60
CGLN63
CGLY72
CALA101
CASN102
CALA103
CGLN111
CPHE113
CTRP121
CHIS126

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

site_idPS00170
Number of Residues18
DetailsCSA_PPIASE_1 Cyclophilin-type peptidyl-prolyl cis-trans isomerase signature. YkgScFHRIIpgFMcQGG
ChainResidueDetails
CTYR48-GLY65

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsMOD_RES: N-acetylmethionine => ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
CVAL2
BPHE74
BLYS141
BGLY143
BGLY145
BILE147
BPHE152
BASN33
BGLY35
BLEU37
BPHE42
BTHR63
BGLY65
BGLY67
BVAL69

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylvaline; partial; in Peptidyl-prolyl cis-trans isomerase A, N-terminally processed => ECO:0000269|PubMed:25489052, ECO:0000269|Ref.12, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712
ChainResidueDetails
CASN3
BLYS102
BGLY104
BILE106
BLEU111
AHIS281

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861
ChainResidueDetails
CVAL29
CPHE83

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
CGLY45
CSER77
CVAL132

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
CILE78

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
CGLY94

site_idSWS_FT_FI7
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:25678563, ECO:0007744|PubMed:19608861
ChainResidueDetails
CHIS126

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17742
ChainResidueDetails
CGLU134

site_idSWS_FT_FI9
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CGLY109

site_idSWS_FT_FI10
Number of Residues1
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate
ChainResidueDetails
CVAL29

site_idSWS_FT_FI11
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0007744|PubMed:28112733
ChainResidueDetails
CPHE83

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
AASP121
AHIS151

site_idMCSA1
Number of Residues7
DetailsM-CSA 189
ChainResidueDetails
CARG55electrostatic stabiliser, hydrogen bond donor, steric role
AHIS281metal ligand
CPHE60polar/non-polar interaction, steric role
CGLN63electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
CASN102electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
CPHE113polar/non-polar interaction, steric role
CLEU122polar/non-polar interaction, steric role
CHIS126polar/non-polar interaction, steric role
AHIS199metal ligand
AARG254transition state stabiliser

237992

PDB entries from 2025-06-25

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