Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2WIU

Mercury-modified bacterial persistence regulator hipBA

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0000976	molecular_function	transcription cis-regulatory region binding
A	0001217	molecular_function	DNA-binding transcription repressor activity
A	0003677	molecular_function	DNA binding
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005829	cellular_component	cytosol
A	0006355	biological_process	regulation of DNA-templated transcription
A	0022611	biological_process	dormancy process
A	0032993	cellular_component	protein-DNA complex
A	0040008	biological_process	regulation of growth
A	0043565	molecular_function	sequence-specific DNA binding
A	0044010	biological_process	single-species biofilm formation
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0046677	biological_process	response to antibiotic
A	0106310	molecular_function	protein serine kinase activity
A	0110001	cellular_component	toxin-antitoxin complex
B	0000976	molecular_function	transcription cis-regulatory region binding
B	0001046	molecular_function	core promoter sequence-specific DNA binding
B	0001217	molecular_function	DNA-binding transcription repressor activity
B	0003677	molecular_function	DNA binding
B	0005515	molecular_function	protein binding
B	0006351	biological_process	DNA-templated transcription
B	0006355	biological_process	regulation of DNA-templated transcription
B	0032993	cellular_component	protein-DNA complex
B	0040008	biological_process	regulation of growth
B	0042803	molecular_function	protein homodimerization activity
B	0043565	molecular_function	sequence-specific DNA binding
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0110001	cellular_component	toxin-antitoxin complex
C	0000287	molecular_function	magnesium ion binding
C	0000976	molecular_function	transcription cis-regulatory region binding
C	0001217	molecular_function	DNA-binding transcription repressor activity
C	0003677	molecular_function	DNA binding
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005829	cellular_component	cytosol
C	0006355	biological_process	regulation of DNA-templated transcription
C	0022611	biological_process	dormancy process
C	0032993	cellular_component	protein-DNA complex
C	0040008	biological_process	regulation of growth
C	0043565	molecular_function	sequence-specific DNA binding
C	0044010	biological_process	single-species biofilm formation
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0046677	biological_process	response to antibiotic
C	0106310	molecular_function	protein serine kinase activity
C	0110001	cellular_component	toxin-antitoxin complex
D	0000976	molecular_function	transcription cis-regulatory region binding
D	0001046	molecular_function	core promoter sequence-specific DNA binding
D	0001217	molecular_function	DNA-binding transcription repressor activity
D	0003677	molecular_function	DNA binding
D	0005515	molecular_function	protein binding
D	0006351	biological_process	DNA-templated transcription
D	0006355	biological_process	regulation of DNA-templated transcription
D	0032993	cellular_component	protein-DNA complex
D	0040008	biological_process	regulation of growth
D	0042803	molecular_function	protein homodimerization activity
D	0043565	molecular_function	sequence-specific DNA binding
D	0045892	biological_process	negative regulation of DNA-templated transcription
D	0110001	cellular_component	toxin-antitoxin complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE HG A 1438

Chain	Residue
A	TRP117
A	CYS168

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG A 1439

Chain	Residue
A	CYS256
A	PRO262
A	LYS266

site_id	AC3
Number of Residues	1
Details	BINDING SITE FOR RESIDUE HG C 1438

Chain	Residue
C	CYS168

site_id	AC4
Number of Residues	1
Details	BINDING SITE FOR RESIDUE HG C 1439

Chain	Residue
C	CYS168

site_id	AC5
Number of Residues	1
Details	BINDING SITE FOR RESIDUE HG C 1440

Chain	Residue
C	CYS256

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE HG B 1087

Chain	Residue
B	LEU70
B	CYS71
B	CL1089
B	THR69

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE HG D 1087

Chain	Residue
D	THR69
D	CYS71
D	CL1088

site_id	AC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 1440

Chain	Residue
A	LYS363
A	ALA365

site_id	AC9
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 1441

Chain	Residue
A	ARG372
A	HIS373

site_id	BC1
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL C 1441

Chain	Residue
C	GLY274

site_id	BC2
Number of Residues	1
Details	BINDING SITE FOR RESIDUE CL B 1089

Chain	Residue
B	HG1087

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL D 1088

Chain	Residue
D	CYS71
D	HG1087

site_id	BC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE CL A 1442

Chain	Residue
A	GLY274
A	ARG277

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	52
Details	DNA_BIND: H-T-H motif => ECO:0000255\|PROSITE-ProRule:PRU00257, ECO:0000269\|PubMed:19150849

Chain	Residue	Details
B	ARG21-ASN47
D	ARG21-ASN47

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305\|PubMed:17041039

Chain	Residue	Details
A	ASP309
C	ASP309

site_id	SWS_FT_FI3
Number of Residues	8
Details	BINDING: BINDING => ECO:0000269\|PubMed:22999936, ECO:0007744\|PDB:3DNT, ECO:0007744\|PDB:3FBR, ECO:0007744\|PDB:3HZI, ECO:0007744\|PDB:3TPT

Chain	Residue	Details
A	ALA152
A	GLU234
A	HIS311
A	TYR331
C	ALA152
C	GLU234
C	HIS311
C	TYR331

site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269\|PubMed:22999936, ECO:0007744\|PDB:3DNT, ECO:0007744\|PDB:3HZI, ECO:0007744\|PDB:3TPT

Chain	Residue	Details
A	LYS181
C	LYS181

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269\|PubMed:17041039, ECO:0000269\|PubMed:22999936

Chain	Residue	Details
A	SER150
C	SER150

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