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1CM4

Motions of calmodulin-four-conformer refinement

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP20
AASP22
AGLY23
AASP24
ATHR26
AGLU31

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 402
ChainResidue
AASP24
ATHR26
AILE27
AGLU31
AHOH538
AASP20
AASP22
AGLY23

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 403
ChainResidue
AASP20
AASP22
AGLY23
AASP24
ATHR26
AILE27
AGLU31
AHOH538

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA A 404
ChainResidue
AASP20
AASP22
AGLY23
AASP24
ATHR26
AGLU31
AHOH538

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 405
ChainResidue
AASP56
AALA57
AASP58
AGLY59
AASN60
ATHR62
AGLU67
AHOH541

site_idAC6
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 406
ChainResidue
AASP56
AALA57
AASP58
AASN60
ATHR62
AASP64
AGLU67
AHOH541

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 407
ChainResidue
AASP56
AALA57
AASP58
AASN60
ATHR62
AASP64
AGLU67
AHOH541

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 408
ChainResidue
AASP56
AALA57
AASP58
AASN60
ATHR62
AGLU67

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 409
ChainResidue
AASP93
AASP95
AASN97
ATYR99
AGLU104
AHOH511

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 410
ChainResidue
AASP93
AASP95
AASN97
ATYR99
AGLU104
AHOH511

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE CA A 411
ChainResidue
AASN97
ATYR99
AILE100
ASER101
AGLU104
AGLN135
AHOH511
AHOH512

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 412
ChainResidue
AASP93
AASP95
AASN97
ATYR99
AGLU104
AHOH511

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 413
ChainResidue
AASP129
AASP131
AASP133
AGLN135
AGLU140
AHOH531

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 414
ChainResidue
AASP129
AASP131
AASP133
AGLN135
AGLU140
AHOH531

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 415
ChainResidue
AASP133
AGLN135
AGLU140
AHOH531
AASP129
AASP131

site_idBC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 416
ChainResidue
AASP129
AASP133
AGLN135
AGLU140
AHOH531

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 417
ChainResidue
AASP133
AASP133
AGLN135
AGLN135

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 Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P0DP23","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
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

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