5ER4

Crystal Structure of Calcium-loaded S100B bound to SC0025

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0001726	cellular_component	ruffle
X	0005509	molecular_function	calcium ion binding
X	0005515	molecular_function	protein binding
X	0005576	cellular_component	extracellular region
X	0005615	cellular_component	extracellular space
X	0005634	cellular_component	nucleus
X	0005654	cellular_component	nucleoplasm
X	0005737	cellular_component	cytoplasm
X	0005829	cellular_component	cytosol
X	0006417	biological_process	regulation of translation
X	0007155	biological_process	cell adhesion
X	0007409	biological_process	axonogenesis
X	0007611	biological_process	learning or memory
X	0008270	molecular_function	zinc ion binding
X	0008284	biological_process	positive regulation of cell population proliferation
X	0016310	biological_process	phosphorylation
X	0019210	molecular_function	kinase inhibitor activity
X	0042802	molecular_function	identical protein binding
X	0042803	molecular_function	protein homodimerization activity
X	0043025	cellular_component	neuronal cell body
X	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
X	0044548	molecular_function	S100 protein binding
X	0045666	biological_process	positive regulation of neuron differentiation
X	0045917	biological_process	positive regulation of complement activation
X	0046872	molecular_function	metal ion binding
X	0048143	biological_process	astrocyte activation
X	0048156	molecular_function	tau protein binding
X	0048306	molecular_function	calcium-dependent protein binding
X	0048471	cellular_component	perinuclear region of cytoplasm
X	0050786	molecular_function	RAGE receptor binding
X	0071638	biological_process	negative regulation of monocyte chemotactic protein-1 production
X	0097490	biological_process	sympathetic neuron projection extension
X	1990138	biological_process	neuron projection extension
X	1990845	biological_process	adaptive thermogenesis

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue CA X 101

Chain	Residue
X	SER18
X	GLU21
X	ASP23
X	LYS26
X	GLU31
X	HOH226

---

site_id	AC2
Number of Residues	6
Details	binding site for residue CA X 102

Chain	Residue
X	GLU67
X	GLU72
X	HOH220
X	ASP61
X	ASP63
X	ASP65

---

site_id	AC3
Number of Residues	6
Details	binding site for residue 5RL X 103

Chain	Residue
X	ASP12
X	CYS84
X	HIS85
X	PHE88
X	PHE88
X	HOH208

---

site_id	AC4
Number of Residues	8
Details	binding site for residue CA X 104

Chain	Residue
X	HOH248
X	HOH248
X	HOH262
X	HOH262
X	HOH266
X	HOH266
X	HOH272
X	HOH272

---

Functional Information from PROSITE/UniProt

site_id	PS00018
Number of Residues	13
Details	EF_HAND_1 EF-hand calcium-binding domain. DSDGDGECDfqEF

Chain	Residue	Details
X	ASP61-PHE73

---

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

Chain	Residue	Details
X	VAL56-VAL77

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	35
Details	Domain: {"description":"EF-hand 1","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	35
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	6
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P04271","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"4026304","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---