Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4IBU

Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R in sequence-specific complex with DNA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000976	molecular_function	transcription cis-regulatory region binding
A	0003677	molecular_function	DNA binding
A	0003700	molecular_function	DNA-binding transcription factor activity
A	0005634	cellular_component	nucleus
A	0006355	biological_process	regulation of DNA-templated transcription
A	0006915	biological_process	apoptotic process
B	0000976	molecular_function	transcription cis-regulatory region binding
B	0003677	molecular_function	DNA binding
B	0003700	molecular_function	DNA-binding transcription factor activity
B	0005634	cellular_component	nucleus
B	0006355	biological_process	regulation of DNA-templated transcription
B	0006915	biological_process	apoptotic process
C	0000976	molecular_function	transcription cis-regulatory region binding
C	0003677	molecular_function	DNA binding
C	0003700	molecular_function	DNA-binding transcription factor activity
C	0005634	cellular_component	nucleus
C	0006355	biological_process	regulation of DNA-templated transcription
C	0006915	biological_process	apoptotic process
D	0000976	molecular_function	transcription cis-regulatory region binding
D	0003677	molecular_function	DNA binding
D	0003700	molecular_function	DNA-binding transcription factor activity
D	0005634	cellular_component	nucleus
D	0006355	biological_process	regulation of DNA-templated transcription
D	0006915	biological_process	apoptotic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 301

Chain	Residue
A	CYS176
A	HIS179
A	CYS238
A	CYS242

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO A 302

Chain	Residue
A	LYS120
A	ARG280
A	HOH434
A	HOH462

site_id	AC3
Number of Residues	11
Details	BINDING SITE FOR RESIDUE EDO A 303

Chain	Residue
A	SER240
A	ARG248
A	ARG249
A	PRO250
A	ILE251
A	GLU271
A	VAL272
A	CYS273
A	HOH454
A	HOH543
A	LYS132

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 304

Chain	Residue
A	LEU130
A	ASN131
A	GLU271
B	SER95
B	SER96

site_id	AC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO A 305

Chain	Residue
A	ALA138
A	ASP184

site_id	AC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 306

Chain	Residue
A	LEU206
A	ASP208
A	ARG209
A	HOH654
C	SER116
F	DG12
F	HOH113

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	CYS176
B	HIS179
B	CYS238
B	CYS242

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 302

Chain	Residue
B	LEU114
B	PRO142
B	HIS233
B	HOH459
B	HOH543

site_id	AC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO B 303

Chain	Residue
B	ALA138
B	HOH454
B	HOH497
B	HOH577

site_id	BC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 304

Chain	Residue
B	SER185
B	ACT305
B	HOH561
D	GLY199
D	ASN200
D	GLU221
D	HOH445
D	HOH519

site_id	BC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE ACT B 305

Chain	Residue
B	SER183
B	ASP184
B	SER185
B	EDO304
B	HOH547
B	HOH561
D	HOH507

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	CYS176
C	HIS179
C	CYS238
C	CYS242

site_id	BC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO C 302

Chain	Residue
C	LEU114
C	PRO142
C	HIS233
C	HOH424
C	HOH617

site_id	BC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO C 303

Chain	Residue
C	LEU130
C	LYS132
C	LYS164
C	GLU271
C	GLU285
C	HOH528
C	HOH639

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 304

Chain	Residue
C	LEU130
C	ASN131
C	GLU271
C	HOH528
C	HOH650
D	SER96

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	CYS176
D	HIS179
D	CYS238
D	CYS242

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO D 302

Chain	Residue
B	LYS139
B	HOH413
D	ALA138
D	LYS139
D	THR140
D	GLU198

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 303

Chain	Residue
D	PRO219
D	HOH422
D	HOH451
D	HOH551

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 304

Chain	Residue
D	ASP207
D	HOH411
D	PRO190
D	TYR205

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 305

Chain	Residue
D	LEU114
D	PRO142
D	THR231
D	HIS233
D	HOH446

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 306

Chain	Residue
B	GLY187
B	LEU188
B	HOH537
D	LEU201
D	ARG202

site_id	CC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE ACT H 101

Chain	Residue
A	SER260
A	SER261
A	HOH580
C	ALA119
C	LYS120
H	DG2

Functional Information from PROSITE/UniProt

site_id	PS00348
Number of Residues	13
Details	P53 p53 family signature. MCNSSCMGGMNRR

Chain	Residue	Details
A	MET237-ARG249

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	190
Details	DNA binding: {"evidences":[{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18996393","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	492
Details	Region: {"description":"Required for interaction with FBXO42","evidences":[{"source":"PubMed","id":"19509332","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	176
Details	Region: {"description":"Interaction with AXIN1","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	28
Details	Region: {"description":"Interaction with the 53BP2 SH3 domain"}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	28
Details	Region: {"description":"Interaction with DNA"}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"PubMed","id":"14534297","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17015838","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18650397","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19515728","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20142040","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Site: {"description":"Interaction with DNA","evidences":[{"source":"PubMed","id":"16793544","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18996393","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20364130","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"N6-lactoyllysine","evidences":[{"source":"PubMed","id":"38653238","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	5
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"19536131","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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