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2LUC

Solution Structure of human S100 calcium-binding protein A11

Functional Information from GO Data
ChainGOidnamespacecontents
A0001726cellular_componentruffle
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005912cellular_componentadherens junction
A0007165biological_processsignal transduction
A0008156biological_processnegative regulation of DNA replication
A0008285biological_processnegative regulation of cell population proliferation
A0014911biological_processpositive regulation of smooth muscle cell migration
A0034774cellular_componentsecretory granule lumen
A0042127biological_processregulation of cell population proliferation
A0042803molecular_functionprotein homodimerization activity
A0044548molecular_functionS100 protein binding
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0070062cellular_componentextracellular exosome
A0098609biological_processcell-cell adhesion
A0098641molecular_functioncadherin binding involved in cell-cell adhesion
B0001726cellular_componentruffle
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005912cellular_componentadherens junction
B0007165biological_processsignal transduction
B0008156biological_processnegative regulation of DNA replication
B0008285biological_processnegative regulation of cell population proliferation
B0014911biological_processpositive regulation of smooth muscle cell migration
B0034774cellular_componentsecretory granule lumen
B0042127biological_processregulation of cell population proliferation
B0042803molecular_functionprotein homodimerization activity
B0044548molecular_functionS100 protein binding
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0070062cellular_componentextracellular exosome
B0098609biological_processcell-cell adhesion
B0098641molecular_functioncadherin binding involved in cell-cell adhesion
Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DTNSDGQLDfsEF
ChainResidueDetails
AASP68-PHE80

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. MMkkLDtnsDgqlDFsEFlnLI
ChainResidueDetails
AMET63-ILE84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues72
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":"N-acetylmethionine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N-acetylalanine; in Protein S100-A11, N-terminally processed","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"18618420","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P50543","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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