3CZT

Crystal Structure of S100B in the Calcium and Zinc Loaded State at pH 9

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0001726	cellular_component	ruffle
X	0005102	molecular_function	signaling receptor binding
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	0007155	biological_process	cell adhesion
X	0007409	biological_process	axonogenesis
X	0007417	biological_process	central nervous system development
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	0008360	biological_process	regulation of cell shape
X	0031643	biological_process	positive regulation of myelination
X	0042802	molecular_function	identical protein binding
X	0042803	molecular_function	protein homodimerization activity
X	0043025	cellular_component	neuronal cell body
X	0043065	biological_process	positive regulation of apoptotic process
X	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
X	0044548	molecular_function	S100 protein binding
X	0045471	biological_process	response to ethanol
X	0045666	biological_process	positive regulation of neuron differentiation
X	0046872	molecular_function	metal ion binding
X	0048156	molecular_function	tau protein binding
X	0048306	molecular_function	calcium-dependent protein binding
X	0048471	cellular_component	perinuclear region of cytoplasm
X	0048708	biological_process	astrocyte differentiation
X	0050786	molecular_function	RAGE receptor binding
X	0050806	biological_process	positive regulation of synaptic transmission
X	0051384	biological_process	response to glucocorticoid
X	0051597	biological_process	response to methylmercury
X	0060291	biological_process	long-term synaptic potentiation
X	0071456	biological_process	cellular response to hypoxia
X	0072347	biological_process	response to anesthetic
X	0097490	biological_process	sympathetic neuron projection extension
X	1990138	biological_process	neuron projection extension
X	1990845	biological_process	adaptive thermogenesis
X	2001015	biological_process	negative regulation of skeletal muscle cell differentiation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA X 92

Chain	Residue
X	SER18
X	GLU21
X	ASP23
X	LYS26
X	GLU31
X	HOH120

---

site_id	AC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA X 93

Chain	Residue
X	GLU67
X	GLU72
X	HOH104
X	ASP61
X	ASP63
X	ASP65

---

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA X 94

Chain	Residue
X	HOH126
X	HOH135
X	HOH161
X	HOH187

---

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN X 95

Chain	Residue
X	HIS15
X	HIS25
X	HIS85
X	HIS90

---

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA X 92

Chain	Residue
X	SER18
X	GLU21
X	ASP23
X	LYS26
X	GLU31
X	HOH120

---

site_id	AC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA X 93

Chain	Residue
X	ASP61
X	ASP63
X	ASP65
X	GLU67
X	GLU72
X	HOH104

---

site_id	AC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CA X 94

Chain	Residue
X	HOH126
X	HOH126
X	HOH135
X	HOH135
X	HOH161
X	HOH161
X	HOH187
X	HOH187

---

site_id	AC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN X 95

Chain	Residue
X	HIS15
X	HIS25
X	HIS85
X	HIS90

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
X	ASP61-PHE73

---

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

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	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20950652","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CZT","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PubMed","id":"20950652","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CZT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D0Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D10","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20950652","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3CZT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D0Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D10","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20950652","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2H61","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3CZT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D0Y","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3D10","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	Modified residue: {"description":"N-acetylserine; alternate","evidences":[{"source":"UniProtKB","id":"P02638","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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