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5SVE

Structure of Calcineurin in complex with NFATc1 LxVP 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
B0016018molecular_functioncyclosporin A binding
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
B0097720biological_processcalcineurin-mediated signaling
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 FE A 401
ChainResidue
AASP90
AHIS92
AASP118
AZN402
AHOH513
AHOH536

site_idAC2
Number of Residues6
Detailsbinding site for residue ZN A 402
ChainResidue
AHIS281
AFE401
AHOH513
AASP118
AASN150
AHIS199

site_idAC3
Number of Residues5
Detailsbinding site for residue CA B 201
ChainResidue
BASP62
BASP64
BASN66
BGLU68
BGLU73

site_idAC4
Number of Residues5
Detailsbinding site for residue CA B 202
ChainResidue
BASP140
BASP142
BASP144
BARG146
BGLU151

site_idAC5
Number of Residues5
Detailsbinding site for residue CA B 203
ChainResidue
BASP30
BASP32
BSER34
BSER36
BGLU41

site_idAC6
Number of Residues5
Detailsbinding site for residue CA B 204
ChainResidue
BASP99
BASP101
BASP103
BTYR105
BGLU110

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 Residues15
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:8524402, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
ChainResidueDetails
BASP30
BGLU73
BASP140
BASP142
BASP144
BARG146
BGLU151
BASP32
BSER34
BSER36
BGLU41
BASP62
BASP64
BASN66
BGLU68

site_idSWS_FT_FI2
Number of Residues5
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448, ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:17498738, ECO:0000269|PubMed:22343722, ECO:0000269|PubMed:23468591, ECO:0000269|PubMed:26794871, ECO:0000269|PubMed:27974827, ECO:0000269|PubMed:31375679, ECO:0000269|PubMed:8524402, ECO:0000312|PDB:6NUC, ECO:0007744|PDB:1AUI, ECO:0007744|PDB:1M63, ECO:0007744|PDB:1MF8, ECO:0007744|PDB:2P6B, ECO:0007744|PDB:3LL8, ECO:0007744|PDB:4F0Z, ECO:0007744|PDB:4OR9, ECO:0007744|PDB:4ORA, ECO:0007744|PDB:4ORC, ECO:0007744|PDB:5SVE
ChainResidueDetails
BASP99
BASP101
BASP103
BTYR105
BGLU110
AHIS281

site_idSWS_FT_FI3
Number of Residues2
DetailsSITE: Interaction with PxVP motif in substrates of the catalytic subunit => ECO:0000269|PubMed:23468591
ChainResidueDetails
BMET117
BASN121

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q63810
ChainResidueDetails
BTYR105

site_idSWS_FT_FI5
Number of Residues1
DetailsLIPID: N-myristoyl glycine => ECO:0000269|PubMed:25255805
ChainResidueDetails
BGLY1

Catalytic Information from CSA
site_idMCSA1
Number of Residues10
DetailsM-CSA 406
ChainResidueDetails
AASP90metal ligand
AHIS281metal ligand
AHIS92metal ligand
AASP118metal ligand
AASP121electrostatic stabiliser
AARG122transition state stabiliser
AASN150metal ligand
AHIS151proton shuttle (general acid/base)
AHIS199metal ligand
AARG254transition state stabiliser

220113

PDB entries from 2024-05-22

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