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CRYSTAL STRUCTURE OF CALCIUM BOUND HUMAN S100A6

Functional Information from GO Data
ChainGOidnamespacecontents
A0001726cellular_componentruffle
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005523molecular_functiontropomyosin binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005635cellular_componentnuclear envelope
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0007165biological_processsignal transduction
A0007409biological_processaxonogenesis
A0008270molecular_functionzinc ion binding
A0009898cellular_componentcytoplasmic side of plasma membrane
A0015075molecular_functionmonoatomic ion transmembrane transporter activity
A0031012cellular_componentextracellular matrix
A0034220biological_processmonoatomic ion transmembrane transport
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0044548molecular_functionS100 protein binding
A0046872molecular_functionmetal ion binding
A0048146biological_processpositive regulation of fibroblast proliferation
A0048306molecular_functioncalcium-dependent protein binding
A0048471cellular_componentperinuclear region of cytoplasm
A0070062cellular_componentextracellular exosome
B0001726cellular_componentruffle
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005523molecular_functiontropomyosin binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007409biological_processaxonogenesis
B0008270molecular_functionzinc ion binding
B0009898cellular_componentcytoplasmic side of plasma membrane
B0015075molecular_functionmonoatomic ion transmembrane transporter activity
B0031012cellular_componentextracellular matrix
B0034220biological_processmonoatomic ion transmembrane transport
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0044548molecular_functionS100 protein binding
B0046872molecular_functionmetal ion binding
B0048146biological_processpositive regulation of fibroblast proliferation
B0048306molecular_functioncalcium-dependent protein binding
B0048471cellular_componentperinuclear region of cytoplasm
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 300
ChainResidue
ASER20
AGLU23
AASP25
ATHR28
AGLU33
AHOH409

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA A 400
ChainResidue
AGLU67
AGLU72
AHOH401
AASP61
AASN63
AASP65

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 300
ChainResidue
BSER20
BGLU23
BASP25
BTHR28
BGLU33
BHOH402

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 400
ChainResidue
BASP61
BASN63
BASP65
BGLU67
BGLU72
BHOH416

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BME A 100
ChainResidue
ACYS3
AHOH452
BLYS40

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME B 200
ChainResidue
ALYS40
BCYS3

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. LMedLDrnkDqevNFqEYvtFL
ChainResidueDetails
ALEU56-LEU77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues70
DetailsDomain: {"description":"EF-hand 1","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues70
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14069","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246905

PDB entries from 2025-12-31

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