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3C1V

The 1.5 A Crystal structure of Ca2+-bound S100A4

Functional Information from GO Data
ChainGOidnamespacecontents
A0001837biological_processepithelial to mesenchymal transition
A0003723molecular_functionRNA binding
A0003779molecular_functionactin binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0042056molecular_functionchemoattractant activity
A0042802molecular_functionidentical protein binding
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0050786molecular_functionRAGE receptor binding
A0050918biological_processpositive chemotaxis
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
B0001837biological_processepithelial to mesenchymal transition
B0003723molecular_functionRNA binding
B0003779molecular_functionactin binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0042056molecular_functionchemoattractant activity
B0042802molecular_functionidentical protein binding
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0048471cellular_componentperinuclear region of cytoplasm
B0050786molecular_functionRAGE receptor binding
B0050918biological_processpositive chemotaxis
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
C0001837biological_processepithelial to mesenchymal transition
C0003723molecular_functionRNA binding
C0003779molecular_functionactin binding
C0005509molecular_functioncalcium ion binding
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005615cellular_componentextracellular space
C0005634cellular_componentnucleus
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0042056molecular_functionchemoattractant activity
C0042802molecular_functionidentical protein binding
C0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
C0046872molecular_functionmetal ion binding
C0046914molecular_functiontransition metal ion binding
C0048306molecular_functioncalcium-dependent protein binding
C0048471cellular_componentperinuclear region of cytoplasm
C0050786molecular_functionRAGE receptor binding
C0050918biological_processpositive chemotaxis
C0062023cellular_componentcollagen-containing extracellular matrix
C0070062cellular_componentextracellular exosome
D0001837biological_processepithelial to mesenchymal transition
D0003723molecular_functionRNA binding
D0003779molecular_functionactin binding
D0005509molecular_functioncalcium ion binding
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005615cellular_componentextracellular space
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0042056molecular_functionchemoattractant activity
D0042802molecular_functionidentical protein binding
D0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
D0046872molecular_functionmetal ion binding
D0046914molecular_functiontransition metal ion binding
D0048306molecular_functioncalcium-dependent protein binding
D0048471cellular_componentperinuclear region of cytoplasm
D0050786molecular_functionRAGE receptor binding
D0050918biological_processpositive chemotaxis
D0062023cellular_componentcollagen-containing extracellular matrix
D0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 102
ChainResidue
DASP63
DASN65
DASP67
DGLU69
DGLU74

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA D 103
ChainResidue
DGLU33
DSER20
DGLU23
DASP25
DLYS28

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 102
ChainResidue
BSER20
BGLU23
BASP25
BLYS28
BGLU33

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 103
ChainResidue
BASP63
BASN65
BASP67
BGLU69
BGLU74

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 102
ChainResidue
CSER20
CGLU23
CASP25
CLYS28
CGLU33

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 103
ChainResidue
CASP63
CASN65
CASP67
CGLU69
CGLU74

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 102
ChainResidue
ASER20
AGLU23
AASP25
ALYS28
AGLU33

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA A 103
ChainResidue
AASP63
AASN65
AASP67
AGLU69
AGLU74

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DSNRDNEVDfqEY
ChainResidueDetails
AASP63-TYR75

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. LMsnLDsnrDnevDFqEYcvFL
ChainResidueDetails
ALEU58-LEU79

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000305
ChainResidueDetails
ALYS28
AGLU33
BLYS28
BGLU33
CLYS28
CGLU33
DLYS28
DGLU33

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00448
ChainResidueDetails
AASP63
BGLU74
CASP63
CASN65
CASP67
CGLU69
CGLU74
DASP63
DASN65
DASP67
DGLU69
AASN65
DGLU74
AASP67
AGLU69
AGLU74
BASP63
BASN65
BASP67
BGLU69

site_idSWS_FT_FI3
Number of Residues4
DetailsMOD_RES: N-acetylalanine => ECO:0000250|UniProtKB:P35466
ChainResidueDetails
AALA2
BALA2
CALA2
DALA2

site_idSWS_FT_FI4
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
ALYS7
ALYS35
BLYS7
BLYS35
CLYS7
CLYS35
DLYS7
DLYS35

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PDB entries from 2024-07-24

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