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4ORA

Crystal structure of a human calcineurin mutant

Functional Information from GO Data
ChainGOidnamespacecontents
A0001913biological_processT cell mediated cytotoxicity
A0001915biological_processnegative regulation of T cell mediated cytotoxicity
A0001946biological_processlymphangiogenesis
A0004721molecular_functionphosphoprotein phosphatase activity
A0004722molecular_functionprotein serine/threonine phosphatase activity
A0004723molecular_functioncalcium-dependent protein serine/threonine phosphatase activity
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005516molecular_functioncalmodulin binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005955cellular_componentcalcineurin complex
A0006468biological_processprotein phosphorylation
A0006470biological_processprotein dephosphorylation
A0007165biological_processsignal transduction
A0007507biological_processheart development
A0007612biological_processlearning
A0007613biological_processmemory
A0008287cellular_componentprotein serine/threonine phosphatase complex
A0010468biological_processregulation of gene expression
A0016311biological_processdephosphorylation
A0016787molecular_functionhydrolase activity
A0017018molecular_functionmyosin phosphatase activity
A0017156biological_processcalcium-ion regulated exocytosis
A0019899molecular_functionenzyme binding
A0023057biological_processnegative regulation of signaling
A0030018cellular_componentZ disc
A0030217biological_processT cell differentiation
A0030315cellular_componentT-tubule
A0030346molecular_functionprotein phosphatase 2B binding
A0031987biological_processlocomotion involved in locomotory behavior
A0033173biological_processcalcineurin-NFAT signaling cascade
A0033192molecular_functioncalmodulin-dependent protein phosphatase activity
A0034097biological_processresponse to cytokine
A0035774biological_processpositive regulation of insulin secretion involved in cellular response to glucose stimulus
A0042098biological_processT cell proliferation
A0042110biological_processT cell activation
A0043029biological_processT cell homeostasis
A0045893biological_processpositive regulation of DNA-templated transcription
A0045944biological_processpositive regulation of transcription by RNA polymerase II
A0046872molecular_functionmetal ion binding
A0046983molecular_functionprotein dimerization activity
A0048167biological_processregulation of synaptic plasticity
A0048675biological_processaxon extension
A0048741biological_processskeletal muscle fiber development
A0050796biological_processregulation of insulin secretion
A0070886biological_processpositive regulation of calcineurin-NFAT signaling cascade
A0097720biological_processcalcineurin-mediated signaling
A0098978cellular_componentglutamatergic synapse
A1900182biological_processpositive regulation of protein localization to nucleus
A1900242biological_processregulation of synaptic vesicle endocytosis
A1905665biological_processpositive regulation of calcium ion import across plasma membrane
A1905673biological_processpositive regulation of lysosome organization
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
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
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
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 Residues5
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
AASP99
AASP127
AASN159
AHIS290
AFE602

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FE A 602
ChainResidue
AGLU490
AZN601
AHOH712
AASP99
AHIS101
AASP127
AHIS290

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 201
ChainResidue
BASP30
BASP32
BSER34
BSER36
BGLU41

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 202
ChainResidue
BASP62
BASP64
BASN66
BGLU68
BGLU73
BHOH309

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 203
ChainResidue
BASP99
BASP101
BASP103
BTYR105
BGLU110
BHOH301

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 204
ChainResidue
BASP140
BASP142
BASP144
BARG146
BGLU151

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
ALEU156-GLU161

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

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

218853

PDB entries from 2024-04-24

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