Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1TCO

TERNARY COMPLEX OF A CALCINEURIN A FRAGMENT, CALCINEURIN B, FKBP12 AND THE IMMUNOSUPPRESSANT DRUG FK506 (TACROLIMUS)

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0033192molecular_functioncalmodulin-dependent protein phosphatase activity
A0097720biological_processcalcineurin-mediated signaling
B0005509molecular_functioncalcium ion binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005955cellular_componentcalcineurin complex
B0008597molecular_functioncalcium-dependent protein serine/threonine phosphatase regulator activity
B0016020cellular_componentmembrane
B0019902molecular_functionphosphatase binding
B0033173biological_processcalcineurin-NFAT signaling cascade
B0042383cellular_componentsarcolemma
B0046872molecular_functionmetal ion binding
C0000413biological_processprotein peptidyl-prolyl isomerization
C0001933biological_processnegative regulation of protein phosphorylation
C0003007biological_processheart morphogenesis
C0003755molecular_functionpeptidyl-prolyl cis-trans isomerase activity
C0005528molecular_functionFK506 binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006936biological_processmuscle contraction
C0007183biological_processobsolete SMAD protein complex assembly
C0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
C0016020cellular_componentmembrane
C0016529cellular_componentsarcoplasmic reticulum
C0016853molecular_functionisomerase activity
C0019221biological_processcytokine-mediated signaling pathway
C0019855molecular_functioncalcium channel inhibitor activity
C0030018cellular_componentZ disc
C0031000biological_processresponse to caffeine
C0031398biological_processpositive regulation of protein ubiquitination
C0032092biological_processpositive regulation of protein binding
C0032515biological_processobsolete negative regulation of phosphoprotein phosphatase activity
C0032880biological_processregulation of protein localization
C0032925biological_processregulation of activin receptor signaling pathway
C0033017cellular_componentsarcoplasmic reticulum membrane
C0042098biological_processT cell proliferation
C0042110biological_processT cell activation
C0042803molecular_functionprotein homodimerization activity
C0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
C0044325molecular_functiontransmembrane transporter binding
C0046332molecular_functionSMAD binding
C0048185molecular_functionactivin binding
C0050776biological_processregulation of immune response
C0051209biological_processrelease of sequestered calcium ion into cytosol
C0051280biological_processnegative regulation of release of sequestered calcium ion into cytosol
C0055010biological_processventricular cardiac muscle tissue morphogenesis
C0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
C0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
C0060347biological_processheart trabecula formation
C0070062cellular_componentextracellular exosome
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 PDB Data
site_id506
Number of Residues18
DetailsTHE FK506 BINDING SITE ON FKBP12 (SUBUNIT C) AS WELL AS FK506 CONTACTS MADE TO CALCINEURIN-A (SUBUNIT A) AND CALCINEURIN-B (SUBUNIT B).
ChainResidue
ATRP352
CPHE46
CGLU54
CVAL55
CILE56
CTRP59
CHIS87
CILE91
CTYR82
CPHE99
ASER353
APHE356
BLEU115
BMET118
BVAL119
CTYR26
CPHE36
CASP37

site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 501
ChainResidue
BASP30
BASP32
BSER34
BSER36
BGLU41

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 502
ChainResidue
BASP62
BASP64
BASN66
BGLU68
BGLU73

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 503
ChainResidue
BASP99
BASP101
BASP103
BTYR105
BGLU110
BHOH619

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 504
ChainResidue
BASP140
BASP142
BASP144
BARG146
BGLU151
BHOH636

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE ZN A 505
ChainResidue
AASP90
AASP118
AASN150
AHIS199
AHIS281
AFE506
APO4507

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 506
ChainResidue
AASP90
AHIS92
AASP118
AZN505
APO4507

site_idAC7
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PO4 A 507
ChainResidue
AHIS92
AASP118
AARG122
AASN150
AHIS151
AARG254
AHIS281
ATYR311
AZN505
AFE506
AHOH524
AHOH663

site_idAC8
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MYR B 508
ChainResidue
ALYS323
AGLU325
AASN326
AVAL328
AASN330
BGLY1
BALA16
BILE19
BLYS20
BGLY35
BPHE71

site_idAC9
Number of Residues19
DetailsBINDING SITE FOR RESIDUE FK5 C 509
ChainResidue
ATRP352
ASER353
APHE356
BHOH516
CTYR26
CPHE36
CASP37
CARG42
CPHE46
CVAL55
CILE56
CTRP59
CALA81
CTYR82
CHIS87
CILE91
CPHE99
CHOH511
CHOH520

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 Residues284
DetailsRegion: {"description":"Catalytic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues9
DetailsRegion: {"description":"Interaction with PxIxIF motif in substrate","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues28
DetailsRegion: {"description":"Calcineurin B binding","evidences":[{"source":"PubMed","id":"16411749","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsMotif: {"description":"SAPNY motif","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"7543369","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TCO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsSite: {"description":"Interaction with PxVP motif in substrate","evidences":[{"source":"UniProtKB","id":"Q08209","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P63328","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues28
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues35
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues5
DetailsRegion: {"description":"Calcineurin A binding","evidences":[{"source":"PubMed","id":"7543369","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"7543369","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1TCO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsSite: {"description":"Interaction with PxVP motif in substrates of the catalytic subunit","evidences":[{"source":"UniProtKB","id":"P63098","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q63810","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues1
DetailsLipidation: {"description":"N-myristoyl glycine","evidences":[{"source":"PubMed","id":"6321184","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues88
DetailsDomain: {"description":"PPIase FKBP-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU00277","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P26883","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1aui
ChainResidueDetails
CILE56
CTYR82
CASP37

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

239149

PDB entries from 2025-07-23

PDB statisticsPDBj update infoContact PDBjnumon