Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

4IBZ

Human p53 core domain with hot spot mutation R273C and second-site suppressor mutation T284R

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	2
Details	BINDING SITE FOR RESIDUE EDO A 302

Chain	Residue
A	THR170
A	VAL172

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO A 303

Chain	Residue
A	ILE254
A	THR256
A	HOH433
A	HOH439
A	ARG158
A	ALA159
A	MET160

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 304

Chain	Residue
A	ASP186
A	ARG196
A	VAL197
A	GLU198
A	ASN235
A	MET237

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

Chain	Residue
A	THR102
A	HOH555

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 301

Chain	Residue
B	CYS176
B	HIS179
B	CYS238
B	CYS242

site_id	AC7
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 302

Chain	Residue
B	SER260
B	SER261
B	HOH529
D	ALA119
D	LYS120
D	HOH435

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 303

Chain	Residue
B	ASP207
B	HOH470
B	HOH506
D	LEU114
D	HIS115

site_id	AC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE EDO B 304

Chain	Residue
B	PRO190
B	PRO191
B	GLN192
B	HIS193
B	ASP207
B	HIS214
B	HOH456
D	HIS115

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO B 305

Chain	Residue
B	PHE113
B	HIS115
B	GLN144
B	HOH541
D	EDO302
D	EDO306

site_id	BC2
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO B 306

Chain	Residue
B	MET160
B	LEU206
B	ASP208
B	THR211
B	ARG213
B	HIS214
B	SER215
B	HOH503
B	HOH562

site_id	BC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ACT B 307

Chain	Residue
B	ARG110
B	HOH505
D	EDO302
D	EDO307

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 301

Chain	Residue
C	CYS176
C	HIS179
C	CYS238
C	CYS242

site_id	BC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 302

Chain	Residue
C	PRO98
C	ARG158
C	MET160
C	ILE254
C	THR256
C	HOH437

site_id	BC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO C 303

Chain	Residue
A	LEU114
A	HIS115
A	SER116
C	ASP207
C	ARG209
C	HOH496

site_id	BC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO C 304

Chain	Residue
A	ALA119
C	SER261
C	GLY262
C	HOH467

site_id	BC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO C 305

Chain	Residue
C	ARG209
C	ASN210

site_id	BC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 301

Chain	Residue
D	CYS176
D	HIS179
D	CYS238
D	CYS242

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 302

Chain	Residue
B	HIS115
B	TRP146
B	EDO305
B	ACT307
D	PRO191
D	GLN192
D	EDO307

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 303

Chain	Residue
D	THR125
D	TYR126
D	HOH434
D	HOH527
D	LEU114
D	SER116
D	CYS124

site_id	CC3
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO D 304

Chain	Residue
D	SER240
D	ARG248
D	CYS273

site_id	CC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE EDO D 305

Chain	Residue
D	MET160
D	LEU206
D	ASP208
D	THR211
D	ARG213
D	HIS214
D	SER215
D	HOH442
D	HOH520

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO D 306

Chain	Residue
B	LEU114
B	HIS115
B	EDO305
D	ASP207
D	HOH432

site_id	CC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE EDO D 307

Chain	Residue
B	TRP146
B	ACT307
D	GLU180
D	PRO191
D	EDO302
D	HOH526
D	HOH541

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE ACT D 308

Chain	Residue
D	GLY187
D	HOH450
D	HOH482

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	246
Details	Region: {"description":"Required for interaction with FBXO42","evidences":[{"source":"PubMed","id":"19509332","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	28
Details	Region: {"description":"Interaction with the 53BP2 SH3 domain"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	28
Details	Region: {"description":"Interaction with DNA"}

Chain

Residue

Details

site_id	SWS_FT_FI4
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_FI5
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_FI6
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_FI7
Number of Residues	7
Details	Modified residue: {"description":"Phosphoserine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine; by AURKB","evidences":[{"source":"PubMed","id":"20959462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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