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

2F2O

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

Functional Information from GO Data
ChainGOidnamespacecontents
A0000922cellular_componentspindle pole
A0005509molecular_functioncalcium ion binding
A0005513biological_processdetection of calcium ion
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005813cellular_componentcentrosome
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0019904molecular_functionprotein domain specific binding
A0030672cellular_componentsynaptic vesicle membrane
A0032991cellular_componentprotein-containing complex
A0043209cellular_componentmyelin sheath
A0046872molecular_functionmetal ion binding
A0097720biological_processcalcineurin-mediated signaling
B0000922cellular_componentspindle pole
B0005509molecular_functioncalcium ion binding
B0005513biological_processdetection of calcium ion
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0019904molecular_functionprotein domain specific binding
B0030672cellular_componentsynaptic vesicle membrane
B0032991cellular_componentprotein-containing complex
B0043209cellular_componentmyelin sheath
B0046872molecular_functionmetal ion binding
B0097720biological_processcalcineurin-mediated signaling
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1001
ChainResidue
AASP20
AASP22
AASP24
ATHR26
AGLU31
AHOH1050

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1002
ChainResidue
ATHR62
AGLU67
AHOH1085
AASP56
AASP58
AASN60

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1003
ChainResidue
AASP93
AASP95
AASN97
ATYR99
AGLU104
AHOH1006

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 1004
ChainResidue
AASP129
AASP131
AASP133
AGLN135
AGLU140
AHOH1007

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1001
ChainResidue
BASP20
BASP22
BASP24
BTHR26
BGLU31
BHOH1058

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 1002
ChainResidue
BASP56
BASP58
BASN60
BTHR62
BGLU67

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1003
ChainResidue
BASP93
BASP95
BASN97
BTYR99
BGLU104
BHOH1007

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 1004
ChainResidue
BASP129
BASP131
BASP133
BGLN135
BGLU140
BHOH1010

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
AASP20-LEU32
AASP56-PHE68
AASP93-LEU105
AASP129-PHE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues14
DetailsRegion: {"description":"Calmodulin-binding","evidences":[{"source":"PubMed","id":"16411749","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues70
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"PubMed","id":"9716384","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

PDB statisticsPDBj update infoContact PDBjnumon