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1JWD

Ca2+-induced Structural Changes in Calcyclin: High-resolution Solution Structure of Ca2+-bound Calcyclin.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0009898cellular_componentcytoplasmic side of plasma membrane
A0044548molecular_functionS100 protein binding
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0062023cellular_componentcollagen-containing extracellular matrix
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0009898cellular_componentcytoplasmic side of plasma membrane
B0044548molecular_functionS100 protein binding
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0048471cellular_componentperinuclear region of cytoplasm
B0062023cellular_componentcollagen-containing extracellular matrix
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DRNKDQEVNfqEY
ChainResidueDetails
AASP61-TYR73

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. LMddLDrnkDqevNFqEYitFL
ChainResidueDetails
ALEU56-LEU77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ATHR28
AGLU33
BTHR28
BGLU33

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP61
BGLU72
AASN63
AASP65
AGLU67
AGLU72
BASP61
BASN63
BASP65
BGLU67

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06703
ChainResidueDetails
ALYS40
BLYS40

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06703
ChainResidueDetails
ASER46
BSER46

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P14069
ChainResidueDetails
ALYS47
BLYS47

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PDB entries from 2024-10-16

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