Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6T58

Structure determination of the transactivation domain of p53 in complex with S100A4 using annexin A2 as a crystallization chaperone

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001525	biological_process	angiogenesis
A	0001533	cellular_component	cornified envelope
A	0001765	biological_process	membrane raft assembly
A	0001786	molecular_function	phosphatidylserine binding
A	0001837	biological_process	epithelial to mesenchymal transition
A	0001921	biological_process	positive regulation of receptor recycling
A	0002020	molecular_function	protease binding
A	0002091	biological_process	negative regulation of receptor internalization
A	0003723	molecular_function	RNA binding
A	0003779	molecular_function	actin binding
A	0004859	molecular_function	phospholipase inhibitor activity
A	0004867	molecular_function	serine-type endopeptidase inhibitor activity
A	0005509	molecular_function	calcium ion binding
A	0005515	molecular_function	protein binding
A	0005544	molecular_function	calcium-dependent phospholipid binding
A	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
A	0005576	cellular_component	extracellular region
A	0005604	cellular_component	basement membrane
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005654	cellular_component	nucleoplasm
A	0005737	cellular_component	cytoplasm
A	0005765	cellular_component	lysosomal membrane
A	0005768	cellular_component	endosome
A	0005769	cellular_component	early endosome
A	0005811	cellular_component	lipid droplet
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005912	cellular_component	adherens junction
A	0006900	biological_process	vesicle budding from membrane
A	0007155	biological_process	cell adhesion
A	0007160	biological_process	cell-matrix adhesion
A	0008092	molecular_function	cytoskeletal protein binding
A	0009986	cellular_component	cell surface
A	0010756	biological_process	positive regulation of plasminogen activation
A	0012506	cellular_component	vesicle membrane
A	0014823	biological_process	response to activity
A	0016020	cellular_component	membrane
A	0016323	cellular_component	basolateral plasma membrane
A	0016363	cellular_component	nuclear matrix
A	0019834	molecular_function	phospholipase A2 inhibitor activity
A	0030199	biological_process	collagen fibril organization
A	0030324	biological_process	lung development
A	0030496	cellular_component	midbody
A	0031012	cellular_component	extracellular matrix
A	0031340	biological_process	positive regulation of vesicle fusion
A	0031902	cellular_component	late endosome membrane
A	0031982	cellular_component	vesicle
A	0032804	biological_process	negative regulation of low-density lipoprotein particle receptor catabolic process
A	0035578	cellular_component	azurophil granule lumen
A	0035749	cellular_component	myelin sheath adaxonal region
A	0036035	biological_process	osteoclast development
A	0042056	molecular_function	chemoattractant activity
A	0042383	cellular_component	sarcolemma
A	0042470	cellular_component	melanosome
A	0042730	biological_process	fibrinolysis
A	0042789	biological_process	mRNA transcription by RNA polymerase II
A	0042802	molecular_function	identical protein binding
A	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
A	0043220	cellular_component	Schmidt-Lanterman incisure
A	0044090	biological_process	positive regulation of vacuole organization
A	0044548	molecular_function	S100 protein binding
A	0045121	cellular_component	membrane raft
A	0045921	biological_process	positive regulation of exocytosis
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046872	molecular_function	metal ion binding
A	0046914	molecular_function	transition metal ion binding
A	0048306	molecular_function	calcium-dependent protein binding
A	0048471	cellular_component	perinuclear region of cytoplasm
A	0050767	biological_process	regulation of neurogenesis
A	0050786	molecular_function	RAGE receptor binding
A	0050918	biological_process	positive chemotaxis
A	0051051	biological_process	negative regulation of transport
A	0051240	biological_process	positive regulation of multicellular organismal process
A	0070062	cellular_component	extracellular exosome
A	0090575	cellular_component	RNA polymerase II transcription regulator complex
A	0098609	biological_process	cell-cell adhesion
A	0098641	molecular_function	cadherin binding involved in cell-cell adhesion
A	0098797	cellular_component	plasma membrane protein complex
A	1904019	biological_process	epithelial cell apoptotic process
A	1905581	biological_process	positive regulation of low-density lipoprotein particle clearance
A	1905602	biological_process	positive regulation of receptor-mediated endocytosis involved in cholesterol transport
A	1905686	biological_process	positive regulation of plasma membrane repair
A	1990665	cellular_component	AnxA2-p11 complex
A	1990667	cellular_component	PCSK9-AnxA2 complex
B	0001525	biological_process	angiogenesis
B	0001533	cellular_component	cornified envelope
B	0001765	biological_process	membrane raft assembly
B	0001786	molecular_function	phosphatidylserine binding
B	0001837	biological_process	epithelial to mesenchymal transition
B	0001921	biological_process	positive regulation of receptor recycling
B	0002020	molecular_function	protease binding
B	0002091	biological_process	negative regulation of receptor internalization
B	0003723	molecular_function	RNA binding
B	0003779	molecular_function	actin binding
B	0004859	molecular_function	phospholipase inhibitor activity
B	0004867	molecular_function	serine-type endopeptidase inhibitor activity
B	0005509	molecular_function	calcium ion binding
B	0005515	molecular_function	protein binding
B	0005544	molecular_function	calcium-dependent phospholipid binding
B	0005546	molecular_function	phosphatidylinositol-4,5-bisphosphate binding
B	0005576	cellular_component	extracellular region
B	0005604	cellular_component	basement membrane
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005654	cellular_component	nucleoplasm
B	0005737	cellular_component	cytoplasm
B	0005765	cellular_component	lysosomal membrane
B	0005768	cellular_component	endosome
B	0005769	cellular_component	early endosome
B	0005811	cellular_component	lipid droplet
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005912	cellular_component	adherens junction
B	0006900	biological_process	vesicle budding from membrane
B	0007155	biological_process	cell adhesion
B	0007160	biological_process	cell-matrix adhesion
B	0008092	molecular_function	cytoskeletal protein binding
B	0009986	cellular_component	cell surface
B	0010756	biological_process	positive regulation of plasminogen activation
B	0012506	cellular_component	vesicle membrane
B	0014823	biological_process	response to activity
B	0016020	cellular_component	membrane
B	0016323	cellular_component	basolateral plasma membrane
B	0016363	cellular_component	nuclear matrix
B	0019834	molecular_function	phospholipase A2 inhibitor activity
B	0030199	biological_process	collagen fibril organization
B	0030324	biological_process	lung development
B	0030496	cellular_component	midbody
B	0031012	cellular_component	extracellular matrix
B	0031340	biological_process	positive regulation of vesicle fusion
B	0031902	cellular_component	late endosome membrane
B	0031982	cellular_component	vesicle
B	0032804	biological_process	negative regulation of low-density lipoprotein particle receptor catabolic process
B	0035578	cellular_component	azurophil granule lumen
B	0035749	cellular_component	myelin sheath adaxonal region
B	0036035	biological_process	osteoclast development
B	0042056	molecular_function	chemoattractant activity
B	0042383	cellular_component	sarcolemma
B	0042470	cellular_component	melanosome
B	0042730	biological_process	fibrinolysis
B	0042789	biological_process	mRNA transcription by RNA polymerase II
B	0042802	molecular_function	identical protein binding
B	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
B	0043220	cellular_component	Schmidt-Lanterman incisure
B	0044090	biological_process	positive regulation of vacuole organization
B	0044548	molecular_function	S100 protein binding
B	0045121	cellular_component	membrane raft
B	0045921	biological_process	positive regulation of exocytosis
B	0045944	biological_process	positive regulation of transcription by RNA polymerase II
B	0046872	molecular_function	metal ion binding
B	0046914	molecular_function	transition metal ion binding
B	0048306	molecular_function	calcium-dependent protein binding
B	0048471	cellular_component	perinuclear region of cytoplasm
B	0050767	biological_process	regulation of neurogenesis
B	0050786	molecular_function	RAGE receptor binding
B	0050918	biological_process	positive chemotaxis
B	0051051	biological_process	negative regulation of transport
B	0051240	biological_process	positive regulation of multicellular organismal process
B	0070062	cellular_component	extracellular exosome
B	0090575	cellular_component	RNA polymerase II transcription regulator complex
B	0098609	biological_process	cell-cell adhesion
B	0098641	molecular_function	cadherin binding involved in cell-cell adhesion
B	0098797	cellular_component	plasma membrane protein complex
B	1904019	biological_process	epithelial cell apoptotic process
B	1905581	biological_process	positive regulation of low-density lipoprotein particle clearance
B	1905602	biological_process	positive regulation of receptor-mediated endocytosis involved in cholesterol transport
B	1905686	biological_process	positive regulation of plasma membrane repair
B	1990665	cellular_component	AnxA2-p11 complex
B	1990667	cellular_component	PCSK9-AnxA2 complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue GOL A 601

Chain	Residue
A	CYS359
A	ARG361
A	ARG405
A	LEU485
A	LYS492

site_id	AC2
Number of Residues	5
Details	binding site for residue GOL A 602

Chain	Residue
A	VAL524
A	PRO332
A	ASP336
A	GLU365
A	SER520

site_id	AC3
Number of Residues	5
Details	binding site for residue CA A 603

Chain	Residue
A	ASP124
A	ASN126
A	ASP128
A	GLU130
A	GLU135

site_id	AC4
Number of Residues	4
Details	binding site for residue CA A 604

Chain	Residue
A	GLY428
A	ARG431
A	GLY433
A	GLU473

site_id	AC5
Number of Residues	3
Details	binding site for residue CA A 605

Chain	Residue
A	GLY276
A	VAL277
A	GLU279

site_id	AC6
Number of Residues	5
Details	binding site for residue CA A 606

Chain	Residue
A	MET344
A	GLY346
A	LEU347
A	GLY348
A	ASP388

site_id	AC7
Number of Residues	7
Details	binding site for residue CA A 607

Chain	Residue
A	ASP222
A	SER223
A	ASN224
A	ARG225
A	ASP226
A	GLU228
A	GLU233

site_id	AC8
Number of Residues	2
Details	binding site for residue CA A 608

Chain	Residue
A	THR349
A	GLU351

site_id	AC9
Number of Residues	7
Details	binding site for residue CA A 609

Chain	Residue
A	SER179
A	GLU182
A	GLY183
A	ASP184
A	LYS187
A	ASN189
A	GLU192

site_id	AD1
Number of Residues	4
Details	binding site for residue CA A 610

Chain	Residue
A	MET504
A	GLY506
A	GLY508
A	ASP548

site_id	AD2
Number of Residues	4
Details	binding site for residue CA A 611

Chain	Residue
A	LYS314
A	LEU317
A	GLU322
B	ASP296

site_id	AD3
Number of Residues	5
Details	binding site for residue CA A 612

Chain	Residue
A	SER81
A	GLU84
A	ASP86
A	LYS89
A	GLU94

site_id	AD4
Number of Residues	7
Details	binding site for residue GOL B 601

Chain	Residue
B	PRO332
B	ASP336
B	ARG361
B	GLU365
B	SER520
B	ARG521
B	VAL524

site_id	AD5
Number of Residues	5
Details	binding site for residue GOL B 602

Chain	Residue
B	CYS359
B	ARG361
B	ASN363
B	ARG405
B	LYS492

site_id	AD6
Number of Residues	5
Details	binding site for residue CA B 603

Chain	Residue
B	MET504
B	GLY506
B	GLY508
B	THR509
B	ASP548

site_id	AD7
Number of Residues	4
Details	binding site for residue CA B 604

Chain	Residue
B	MET344
B	GLY346
B	GLY348
B	ASP388

site_id	AD8
Number of Residues	1
Details	binding site for residue CA B 605

Chain	Residue
B	SER460

site_id	AD9
Number of Residues	5
Details	binding site for residue CA B 606

Chain	Residue
B	GLY428
B	VAL429
B	ARG431
B	GLY433
B	GLU473

site_id	AE1
Number of Residues	3
Details	binding site for residue CA B 607

Chain	Residue
B	GLY276
B	VAL277
B	GLU279

site_id	AE2
Number of Residues	3
Details	binding site for residue CA B 608

Chain	Residue
B	LYS314
B	LEU317
B	GLU322

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ASP124-TYR136
A	ASP222-TYR234

site_id	PS00223
Number of Residues	53
Details	ANNEXIN_1 Annexin repeat signature. GVdevtivniLtnRsneQrqDiafaYqrrtkkeLasaLksalsGhletvIlgL

Chain	Residue	Details
A	GLY276-LEU328
A	GLY348-LEU400
A	GLY433-LEU485
A	GLY508-LEU560

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

Chain	Residue	Details
A	LEU119-LEU140
A	LEU217-LEU238

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Motif: {"description":"TADI"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	1
Details	Modified residue: {"description":"Phosphothreonine; by CK1, VRK1 and VRK2","evidences":[{"source":"PubMed","id":"10606744","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10951572","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16704422","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"31527692","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CHEK2, CK1 and PLK3","evidences":[{"source":"PubMed","id":"10570149","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11447225","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11551930","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12810724","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20041275","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by MAPKAPK5","evidences":[{"source":"PubMed","id":"17254968","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by CDK5, DYRK2, HIPK2 and PKC/PRKCG","evidences":[{"source":"PubMed","id":"11740489","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11780126","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16377624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17349958","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17591690","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	1
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"21597459","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	142
Details	Repeat: {"description":"Annexin 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	142
Details	Repeat: {"description":"Annexin 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	144
Details	Repeat: {"description":"Annexin 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	142
Details	Repeat: {"description":"Annexin 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01245","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Modified residue: {"description":"Phosphoserine; by PKC","evidences":[{"source":"PubMed","id":"28669632","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2946940","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	2
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P07356","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	35
Details	Domain: {"description":"EF-hand 1","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
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_FI19
Number of Residues	2
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)