1JT0

Crystal structure of a cooperative QacR-DNA complex

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003677	molecular_function	DNA binding
A	0003700	molecular_function	DNA-binding transcription factor activity
A	0045892	biological_process	negative regulation of DNA-templated transcription
B	0003677	molecular_function	DNA binding
B	0003700	molecular_function	DNA-binding transcription factor activity
B	0045892	biological_process	negative regulation of DNA-templated transcription
C	0003677	molecular_function	DNA binding
C	0003700	molecular_function	DNA-binding transcription factor activity
C	0045892	biological_process	negative regulation of DNA-templated transcription
D	0003677	molecular_function	DNA binding
D	0003700	molecular_function	DNA-binding transcription factor activity
D	0045892	biological_process	negative regulation of DNA-templated transcription

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 B 299

Chain	Residue
B	LYS60
B	TYR91

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 D 899

Chain	Residue
D	LYS60
D	TYR91

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 C 699

Chain	Residue
C	LYS60
C	TYR91

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site_id	AC4
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 999

Chain	Residue
A	LYS60
A	TYR91

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site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 B 399

Chain	Residue
B	ASP144
B	HOH402
D	LYS177
B	ASN143

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Functional Information from PROSITE/UniProt

site_id	PS01081
Number of Residues	31
Details	HTH_TETR_1 TetR-type HTH domain signature. GYnatTTgeIvklseSSkGnLYyHFkTKen.L

Chain	Residue	Details
A	GLY19-LEU49

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	76
Details	DNA binding: {"description":"H-T-H motif","evidences":[{"source":"PROSITE-ProRule","id":"PRU00335","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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