2VBW

Feast or famine regulatory protein (Rv3291c)from M. tuberculosis complexed with L-Phenylalanine

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	HTH_AsnC-type	e2vbwA1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: HTH_AsnC-type	ECOD (1.6)
A	AsnC_trans_reg	e2vbwA2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: AsnC_trans_reg	ECOD (1.6)
B	HTH_AsnC-type	e2vbwB1	A: alpha arrays	X: HTH	H: HTH	T: winged	F: HTH_AsnC-type	ECOD (1.6)
B	AsnC_trans_reg	e2vbwB2	A: a+b two layers	X: Alpha-beta plaits	H: Dimeric alpha+beta barrel (From Topology)	T: Dimeric alpha+beta barrel	F: AsnC_trans_reg	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
A	3.30.70.920	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Lrp/AsnC effector binding domain/regulation of amino acid metabolism (RAM) domain	CATH (4.3.0)
B	1.10.10.10	Mainly Alpha	Orthogonal Bundle	Arc Repressor Mutant, subunit A	Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain	CATH (4.3.0)
B	3.30.70.920	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Lrp/AsnC effector binding domain/regulation of amino acid metabolism (RAM) domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01037	Lrp/AsnC ligand binding domain (AsnC_trans_reg)	Lrp/AsnC ligand binding domain	The l-leucine-responsive regulatory protein (Lrp/AsnC) family is a family of similar bacterial transcription regulatory proteins. The family is named after two E. coli proteins involved in regulating amino acid metabolism. This entry corresponds to ...	The l-leucine-responsive regulatory protein (Lrp/AsnC) family is a family of similar bacterial transcription regulatory proteins. The family is named after two E. coli proteins involved in regulating amino acid metabolism. This entry corresponds to the usually C-terminal regulatory ligand binding domain. Structurally this domain has a dimeric alpha/beta barrel fold [2]. This domain binds almost exclusively amino acids but also 4-hydroxyphenylpyruvate and kynurenine (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).	Domain
A, B	PF13412	Winged helix-turn-helix DNA-binding (HTH_24)	Winged helix-turn-helix DNA-binding	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	TRANSCRIPTIONAL REGULATORY PROTEIN	DNA binding binding organic cyclic compound binding nucleic acid binding amino acid binding sequence-specific DNA binding	cellular component organization cellular component biogenesis cellular component assembly protein-containing complex organization protein complex oligomerization protein-containing complex assembly protein homooligomerization cellular process cellular component organization or biogenesis	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036388	Winged helix-like DNA-binding domain superfamily	Homologous Superfamily
A, B	IPR019887	Transcription regulator AsnC/Lrp, ligand binding domain	Domain
A, B	IPR036390	Winged helix DNA-binding domain superfamily	Homologous Superfamily
A, B	IPR000485	AsnC-type HTH domain	Domain
A, B	IPR011008	Dimeric alpha-beta barrel	Homologous Superfamily
A, B	IPR019888	Transcription regulator AsnC-like	Family

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.