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1DEG

THE LINKER OF DES-GLU84 CALMODULIN IS BENT AS SEEN IN THE CRYSTAL STRUCTURE

Functional Information from GO Data
ChainGOidnamespacecontents
A0000922cellular_componentspindle pole
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005819cellular_componentspindle
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
A0019904molecular_functionprotein domain specific binding
A0032991cellular_componentprotein-containing complex
A0046872molecular_functionmetal ion binding
A0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
A0060316biological_processpositive regulation of ryanodine-sensitive calcium-release channel activity
Functional Information from PDB Data
site_idAC1
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 1
ChainResidue
AILE27

site_idAC2
Number of Residues1
DetailsBINDING SITE FOR RESIDUE CA A 3
ChainResidue
AILE100

site_idEF1
Number of Residues12
Details
ChainResidue
AASP20
ATHR29
ALYS30
AGLU31
ALYS21
AASP22
AGLY23
AASP24
AGLY25
ATHR26
AILE27
ATHR28

site_idEF2
Number of Residues12
Details
ChainResidue
AASP56
AALA57
AASP58
AGLY59
AASN60
AGLY61
ATHR62
AILE63
AASP64
APHE65
APRO66
AGLU67

site_idEF3
Number of Residues12
Details
ChainResidue
AASP93
ALYS94
AASP95
AGLY96
AASN97
AGLY98
ATYR99
AILE100
ASER101
AALA102
AALA103
AGLU104

site_idEF4
Number of Residues12
Details
ChainResidue
AASN129
AILE130
AASP131
AGLY132
AASP133
AGLY134
AGLN135
AVAL136
AASN137
ATYR138
AGLU139
AGLU140

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
ALYS21
APHE68
AASP95
AASN97
ATYR99
ASER101
AARG106
AASP131
AASP133
AGLN135
AASN137
AGLY23
AVAL142
AGLY25
AILE27
ALEU32
AALA57
AGLY59
AGLY61
AILE63

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-methyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ATHR117

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AASP22

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine; by CaMK4 => ECO:0000250|UniProtKB:P0DP29
ChainResidueDetails
AGLU45

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AGLU82
AALA103

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
AGLY96

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ASER101
AGLU140

site_idSWS_FT_FI8
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:P0DP23
ChainResidueDetails
ALEU112

site_idSWS_FT_FI9
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate => ECO:0000269|PubMed:9716384
ChainResidueDetails
AASP22

226707

PDB entries from 2024-10-30

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