3Q01

An induced fit mechanism regulates p53 DNA binding kinetics to confer sequence specificity

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
A	0051262	biological_process	protein tetramerization
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
B	0051262	biological_process	protein tetramerization

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1

Chain	Residue
A	CYS176
A	HIS179
A	CYS238
A	CYS242

---

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1

Chain	Residue
B	CYS176
B	HIS179
B	CYS238
B	CYS242

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	MET237-ARG249

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	380
Details	DNA_BIND: DNA_BIND => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130

Chain	Residue	Details
A	THR102-THR322
B	THR102-THR322

---

site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269|PubMed:14534297, ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:17015838, ECO:0000269|PubMed:18650397, ECO:0000269|PubMed:19515728, ECO:0000269|PubMed:20142040, ECO:0000269|PubMed:20364130

Chain	Residue	Details
A	CYS176
A	HIS179
A	CYS238
A	CYS242
B	CYS176
B	HIS179
B	CYS238
B	CYS242

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Interaction with DNA => ECO:0000269|PubMed:16793544, ECO:0000269|PubMed:18996393, ECO:0000269|PubMed:20364130

Chain	Residue	Details
A	LYS120
B	LYS120

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-lactoyllysine => ECO:0000269|PubMed:38653238

Chain	Residue	Details
A	LYS120
A	LYS139
B	LYS120
B	LYS139

---

site_id	SWS_FT_FI5
Number of Residues	4
Details	MOD_RES: Phosphoserine; by AURKB => ECO:0000269|PubMed:20959462

Chain	Residue	Details
A	SER183
A	SER269
B	SER183
B	SER269

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462

Chain	Residue	Details
A	THR284
B	THR284

---

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Symmetric dimethylarginine; by PRMT5 => ECO:0000269|PubMed:19011621

Chain	Residue	Details
A	ARG335
A	ARG337
B	ARG335
B	ARG337

---

site_id	SWS_FT_FI8
Number of Residues	2
Details	MOD_RES: Phosphoserine; by AURKA, CDK1 and CDK2 => ECO:0000269|PubMed:10884347, ECO:0000269|PubMed:14702041

Chain	Residue	Details
A	ASN345
B	ASN345

---

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P02340

Chain	Residue	Details
A	LYS351
B	LYS351

---

site_id	SWS_FT_FI10
Number of Residues	2
Details	MOD_RES: Omega-N-methylarginine; by PRMT5 => ECO:0000269|PubMed:19011621

Chain	Residue	Details
A	ARG333
B	ARG333

---

site_id	SWS_FT_FI11
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19536131

Chain	Residue	Details
A	LYS291
A	THR322
B	LYS291
B	THR322

---

site_id	SWS_FT_FI12
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000269|PubMed:19033443

Chain	Residue	Details
A	LYS351
B	LYS351

---