7YGI

Crystal structure of p53 DBD domain in complex with azurin

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	0005507	molecular_function	copper ion binding
C	0005515	molecular_function	protein binding
C	0008270	molecular_function	zinc ion binding
C	0009055	molecular_function	electron transfer activity
C	0042597	cellular_component	periplasmic space
C	0042802	molecular_function	identical protein binding
C	0046872	molecular_function	metal ion binding
C	0046914	molecular_function	transition metal ion binding
D	0005507	molecular_function	copper ion binding
D	0005515	molecular_function	protein binding
D	0008270	molecular_function	zinc ion binding
D	0009055	molecular_function	electron transfer activity
D	0042597	cellular_component	periplasmic space
D	0042802	molecular_function	identical protein binding
D	0046872	molecular_function	metal ion binding
D	0046914	molecular_function	transition metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS00196
Number of Residues	17
Details	COPPER_BLUE Type-1 copper (blue) proteins signature. GeqYmFFCtfPgHsal.M

Chain	Residue	Details
C	GLY105-MET121

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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	6
Details	BINDING: BINDING => ECO:0000269|PubMed:1420141

Chain	Residue	Details
C	HIS46
C	CYS112
C	HIS117
D	HIS46
D	CYS112
D	HIS117
B	CYS238
B	CYS242

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING:

Chain	Residue	Details
C	MET121
D	MET121

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site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:23431171

Chain	Residue	Details
A	LYS120
B	LYS120

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site_id	SWS_FT_FI4
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

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site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphothreonine; by AURKB => ECO:0000269|PubMed:20959462

Chain	Residue	Details
A	THR284
B	THR284

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