Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

2WCE

calcium-free (apo) S100A12

Functional Information from GO Data
ChainGOidnamespacecontents
A0002548biological_processmonocyte chemotaxis
A0005507molecular_functioncopper ion binding
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0005886cellular_componentplasma membrane
A0006805biological_processxenobiotic metabolic process
A0006954biological_processinflammatory response
A0008270molecular_functionzinc ion binding
A0030593biological_processneutrophil chemotaxis
A0031640biological_processkilling of cells of another organism
A0034774cellular_componentsecretory granule lumen
A0042742biological_processdefense response to bacterium
A0042802molecular_functionidentical protein binding
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043406biological_processpositive regulation of MAP kinase activity
A0043542biological_processendothelial cell migration
A0045087biological_processinnate immune response
A0045576biological_processmast cell activation
A0046872molecular_functionmetal ion binding
A0048306molecular_functioncalcium-dependent protein binding
A0050729biological_processpositive regulation of inflammatory response
A0050786molecular_functionRAGE receptor binding
A0050832biological_processdefense response to fungus
A0051092biological_processpositive regulation of NF-kappaB transcription factor activity
A0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
B0002548biological_processmonocyte chemotaxis
B0005507molecular_functioncopper ion binding
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0005886cellular_componentplasma membrane
B0006805biological_processxenobiotic metabolic process
B0006954biological_processinflammatory response
B0008270molecular_functionzinc ion binding
B0030593biological_processneutrophil chemotaxis
B0031640biological_processkilling of cells of another organism
B0034774cellular_componentsecretory granule lumen
B0042742biological_processdefense response to bacterium
B0042802molecular_functionidentical protein binding
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0043406biological_processpositive regulation of MAP kinase activity
B0043542biological_processendothelial cell migration
B0045087biological_processinnate immune response
B0045576biological_processmast cell activation
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0050729biological_processpositive regulation of inflammatory response
B0050786molecular_functionRAGE receptor binding
B0050832biological_processdefense response to fungus
B0051092biological_processpositive regulation of NF-kappaB transcription factor activity
B0061844biological_processantimicrobial humoral immune response mediated by antimicrobial peptide
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA B 1091
ChainResidue
BSER18
BLYS21
BHIS23
BTHR26
BHOH2049
BHOH2086

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA A 1091
ChainResidue
ATHR26
AHOH2052
AHOH2085
ASER18
ALYS21
AHIS23

Functional Information from PROSITE/UniProt
site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. IFqgLDanqDeqvDFqEFisMV
ChainResidueDetails
AILE56-VAL77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19501594, ECO:0007744|PDB:2WC8, ECO:0007744|PDB:2WCB
ChainResidueDetails
AASP25
AHIS15
BHIS85
BHIS89
AHIS85
AHIS89
BHIS15
BASP25

site_idSWS_FT_FI2
Number of Residues20
DetailsBINDING: BINDING => ECO:0000269|PubMed:11134923, ECO:0000269|PubMed:12777802, ECO:0007744|PDB:1E8A, ECO:0007744|PDB:1ODB
ChainResidueDetails
ALYS21
AHIS23
ATHR26
ASER18
AGLN67
AGLU72
BSER18
BLYS21
BHIS23
BTHR26
BGLU31
BASP61
BASN63
BASP65
BGLN67
BGLU72
AGLU31
AASP61
AASN63
AASP65

220472

PDB entries from 2024-05-29

PDB statisticsPDBj update infoContact PDBjnumon