5ES5

Crystal structure of the initiation module of LgrA in the "open" and "closed " adenylation states

External Resource: Annotation

Domain Annotation: ECOD Classification
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	AMP-binding_3rd	e5es5A2	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_3rd	ECOD (1.6)
A	AMP-binding_C	e5es5A3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_C	ECOD (1.6)
A	Formyl_trans_N	e5es5A5	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
A	AMP-binding_1st	e5es5A1	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_1st	ECOD (1.6)
A	AMP-binding_2nd	e5es5A4	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_2nd	ECOD (1.6)
B	AMP-binding_3rd	e5es5B2	A: beta barrels	X: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	H: beta-barrel domain in acetyl-CoA synthetase-like proteins (From Topology)	T: beta-barrel domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_3rd	ECOD (1.6)
B	AMP-binding_C	e5es5B3	A: a+b two layers	X: Alpha-lytic protease prodomain-like	H: a+b domain in acetyl-CoA synthetase-like proteins (From Topology)	T: a+b domain in acetyl-CoA synthetase-like proteins	F: AMP-binding_C	ECOD (1.6)
B	Formyl_trans_N	e5es5B5	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
B	AMP-binding_1st	e5es5B1	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_1st	ECOD (1.6)
B	AMP-binding_2nd	e5es5B4	A: a/b three-layered sandwiches	X: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	H: Rossmann-like domain in Acetyl-CoA synthetase-like proteins (From Topology)	T: Rossmann-like domain in Acetyl-CoA synthetase-like proteins	F: AMP-binding_2nd	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00501	AMP-binding enzyme (AMP-binding)	AMP-binding enzyme	-	Family
A, B	PF13193	AMP-binding enzyme C-terminal domain (AMP-binding_C)	AMP-binding enzyme C-terminal domain	This is a small domain that is found C terminal to Pfam:PF00501. It has a central beta sheet core that is flanked by alpha helices.	Domain
A, B	PF00551	Formyl transferase (Formyl_trans_N)	Formyl transferase	This family includes the following members. Glycinamide ribonucleotide transformylase catalyses the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces ...	This family includes the following members. Glycinamide ribonucleotide transformylase catalyses the third step in de novo purine biosynthesis, the transfer of a formyl group to 5'-phosphoribosylglycinamide. Formyltetrahydrofolate deformylase produces formate from formyl- tetrahydrofolate. Methionyl-tRNA formyltransferase transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. Inclusion of the following members is supported by PSI-blast. HOXX_BRAJA (P31907) contains a related domain of unknown function. PRTH_PORGI (P46071) contains a related domain of unknown function. Y09P_MYCTU (Q50721) contains a related domain of unknown function.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Linear gramicidin synthetase subunit A	vitamin binding amide binding modified amino acid binding binding phosphopantetheine binding small molecule binding catalytic activity ligase activity	antibiotic metabolic process biosynthetic process metabolic process antibiotic biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR006162	Phosphopantetheine attachment site	PTM
A, B	IPR009081	Phosphopantetheine binding ACP domain	Domain
A, B	IPR010071	Amino acid adenylation domain	Domain
A, B	IPR036477	Formyl transferase, N-terminal domain superfamily	Homologous Superfamily
A, B	IPR020845	AMP-binding, conserved site	Conserved Site
A, B	IPR023213	Chloramphenicol acetyltransferase-like domain superfamily	Homologous Superfamily
A, B	IPR010060	Non-ribosomal peptide synthase	Domain
A, B	IPR045851	AMP-binding enzyme, C-terminal domain superfamily	Homologous Superfamily
A, B	IPR020806	Polyketide synthase, phosphopantetheine-binding domain	Domain
A, B	IPR001242	Condensation domain	Domain
A, B	IPR036736	ACP-like superfamily	Homologous Superfamily
A, B	IPR002376	Formyl transferase, N-terminal	Domain
A, B	IPR025110	AMP-binding enzyme, C-terminal domain	Domain
A, B	IPR000873	AMP-dependent synthetase/ligase domain	Domain

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.