1E8A

The three-dimensional structure of human S100A12

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002376	biological_process	immune system process
A	0002548	biological_process	monocyte chemotaxis
A	0005507	molecular_function	copper ion binding
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0005886	cellular_component	plasma membrane
A	0006805	biological_process	xenobiotic metabolic process
A	0006954	biological_process	inflammatory response
A	0008270	molecular_function	zinc ion binding
A	0016020	cellular_component	membrane
A	0030593	biological_process	neutrophil chemotaxis
A	0031640	biological_process	killing of cells of another organism
A	0034774	cellular_component	secretory granule lumen
A	0042742	biological_process	defense response to bacterium
A	0042802	molecular_function	identical protein binding
A	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
A	0043406	biological_process	positive regulation of MAP kinase activity
A	0043542	biological_process	endothelial cell migration
A	0045087	biological_process	innate immune response
A	0045576	biological_process	mast cell activation
A	0046872	molecular_function	metal ion binding
A	0048306	molecular_function	calcium-dependent protein binding
A	0050729	biological_process	positive regulation of inflammatory response
A	0050786	molecular_function	RAGE receptor binding
A	0050832	biological_process	defense response to fungus
A	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
A	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
B	0002376	biological_process	immune system process
B	0002548	biological_process	monocyte chemotaxis
B	0005507	molecular_function	copper ion binding
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0005886	cellular_component	plasma membrane
B	0006805	biological_process	xenobiotic metabolic process
B	0006954	biological_process	inflammatory response
B	0008270	molecular_function	zinc ion binding
B	0016020	cellular_component	membrane
B	0030593	biological_process	neutrophil chemotaxis
B	0031640	biological_process	killing of cells of another organism
B	0034774	cellular_component	secretory granule lumen
B	0042742	biological_process	defense response to bacterium
B	0042802	molecular_function	identical protein binding
B	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
B	0043406	biological_process	positive regulation of MAP kinase activity
B	0043542	biological_process	endothelial cell migration
B	0045087	biological_process	innate immune response
B	0045576	biological_process	mast cell activation
B	0046872	molecular_function	metal ion binding
B	0048306	molecular_function	calcium-dependent protein binding
B	0050729	biological_process	positive regulation of inflammatory response
B	0050786	molecular_function	RAGE receptor binding
B	0050832	biological_process	defense response to fungus
B	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
B	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1089

Chain	Residue
A	SER18
A	LYS21
A	HIS23
A	THR26
A	GLU31
A	HOH2087

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1090

Chain	Residue
A	GLN67
A	GLU72
A	HOH2084
A	ASP61
A	ASN63
A	ASP65

---

site_id	AC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 1089

Chain	Residue
B	SER18
B	LYS21
B	HIS23
B	THR26
B	GLU31
B	HOH2064

---

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA B 1090

Chain	Residue
B	ASP61
B	ASN63
B	ASP65
B	GLN67
B	GLU72
B	HOH2061

---

Functional Information from PROSITE/UniProt

site_id	PS00303
Number of Residues	22
Details	S100_CABP S-100/ICaBP type calcium binding protein signature. IFqgLDanqDeqvDFqEFisLV

Chain	Residue	Details
A	ILE56-VAL77

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	70
Details	Domain: {"description":"EF-hand 1","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	70
Details	Domain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	30
Details	Region: {"description":"Hinge domain"}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Binding site: {"evidences":[{"source":"PubMed","id":"19501594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2WC8","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2WCB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11134923","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12777802","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E8A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1ODB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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