Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1DT7

SOLUTION STRUCTURE OF THE C-TERMINAL NEGATIVE REGULATORY DOMAIN OF P53 IN A COMPLEX WITH CA2+-BOUND S100B(BB)

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001726	cellular_component	ruffle
A	0005102	molecular_function	signaling receptor binding
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0007155	biological_process	cell adhesion
A	0007611	biological_process	learning or memory
A	0007613	biological_process	memory
A	0008270	molecular_function	zinc ion binding
A	0008284	biological_process	positive regulation of cell population proliferation
A	0008360	biological_process	regulation of cell shape
A	0031643	biological_process	positive regulation of myelination
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0043025	cellular_component	neuronal cell body
A	0043065	biological_process	positive regulation of apoptotic process
A	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
A	0044548	molecular_function	S100 protein binding
A	0045471	biological_process	response to ethanol
A	0045666	biological_process	positive regulation of neuron differentiation
A	0046872	molecular_function	metal ion binding
A	0048156	molecular_function	tau protein binding
A	0048168	biological_process	regulation of neuronal synaptic plasticity
A	0048306	molecular_function	calcium-dependent protein binding
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0048708	biological_process	astrocyte differentiation
A	0050786	molecular_function	RAGE receptor binding
A	0050806	biological_process	positive regulation of synaptic transmission
A	0051384	biological_process	response to glucocorticoid
A	0051597	biological_process	response to methylmercury
A	0060291	biological_process	long-term synaptic potentiation
A	0071456	biological_process	cellular response to hypoxia
A	0072347	biological_process	response to anesthetic
A	0097490	biological_process	sympathetic neuron projection extension
A	1990138	biological_process	neuron projection extension
A	1990845	biological_process	adaptive thermogenesis
A	2001015	biological_process	negative regulation of skeletal muscle cell differentiation
B	0001726	cellular_component	ruffle
B	0005102	molecular_function	signaling receptor binding
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0007155	biological_process	cell adhesion
B	0007611	biological_process	learning or memory
B	0007613	biological_process	memory
B	0008270	molecular_function	zinc ion binding
B	0008284	biological_process	positive regulation of cell population proliferation
B	0008360	biological_process	regulation of cell shape
B	0031643	biological_process	positive regulation of myelination
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0043025	cellular_component	neuronal cell body
B	0043065	biological_process	positive regulation of apoptotic process
B	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
B	0044548	molecular_function	S100 protein binding
B	0045471	biological_process	response to ethanol
B	0045666	biological_process	positive regulation of neuron differentiation
B	0046872	molecular_function	metal ion binding
B	0048156	molecular_function	tau protein binding
B	0048168	biological_process	regulation of neuronal synaptic plasticity
B	0048306	molecular_function	calcium-dependent protein binding
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0048708	biological_process	astrocyte differentiation
B	0050786	molecular_function	RAGE receptor binding
B	0050806	biological_process	positive regulation of synaptic transmission
B	0051384	biological_process	response to glucocorticoid
B	0051597	biological_process	response to methylmercury
B	0060291	biological_process	long-term synaptic potentiation
B	0071456	biological_process	cellular response to hypoxia
B	0072347	biological_process	response to anesthetic
B	0097490	biological_process	sympathetic neuron projection extension
B	1990138	biological_process	neuron projection extension
B	1990845	biological_process	adaptive thermogenesis
B	2001015	biological_process	negative regulation of skeletal muscle cell differentiation

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 114

Chain	Residue
A	SER18
A	ASP23
A	LYS26
A	LEU27
A	GLU31

site_id	AC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA A 115

Chain	Residue
A	ASP65
A	GLU67
A	GLU72
A	ASP61
A	GLU62
A	ASP63
A	GLY64

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA B 116

Chain	Residue
B	SER18
B	ASP23
B	LYS26
B	GLU31

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CA B 117

Chain	Residue
B	ASP61
B	GLU62
B	ASP63
B	GLY64
B	ASP65
B	GLU67
B	GLU72

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP61-PHE73

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

Chain	Residue	Details
A	VAL56-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

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	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14621986","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18949447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2K7O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	10
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"18949447","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2K7O","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"P02638","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	38
Details	Region: {"description":"Basic (repression of DNA-binding)"}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Motif: {"description":"[KR]-[STA]-K motif"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; by SMYD2; alternate","evidences":[{"source":"PubMed","id":"17108971","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22864287","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; by SETD7","evidences":[{"source":"PubMed","id":"15525938","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16415881","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"10656795","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"29474172","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-methyllysine; by KMT5A; alternate","evidences":[{"source":"PubMed","id":"17707234","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20870725","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22864287","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)","evidences":[{"source":"PubMed","id":"11124955","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22214662","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1999","firstPage":"6462","lastPage":"6471","volume":"18","journal":"EMBO J.","title":"Activation of p53 by conjugation to the ubiquitin-like protein SUMO-1.","authors":["Gostissa M.","Hengstermann A.","Fogal V.","Sandy P.","Schwarz S.E.","Scheffner M.","Del Sal G."]}}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)