6MFZ | pdb_00006mfz

Crystal structure of dimodular LgrA in a condensation state

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	e6mfzA11	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	PP-binding	e6mfzA6	A: alpha bundles	X: ACP-like	H: Acyl-carrier protein (ACP) (From Topology)	T: Acyl-carrier protein (ACP)	F: PP-binding	ECOD (1.6)
A	AMP-binding_C	e6mfzA5	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	Condensation_N	e6mfzA8	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Condensation_N	ECOD (1.6)
A	Condensation_C	e6mfzA7	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: Condensation_C	ECOD (1.6)
A	AMP-binding_2nd,AMP-binding_3rd,AMP-binding_C	e6mfzA4	A: a+b complex topology	X: CoA-dependent acyltransferases (From Topology)	H: CoA-dependent acyltransferases (From Topology)	T: CoA-dependent acyltransferases	F: AMP-binding_2nd,AMP-binding_3rd,AMP-binding_C	ECOD (1.6)
A	Formyl_trans_N	e6mfzA1	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	e6mfzA3	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	e6mfzA2	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	e6mfzB1	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	Formyl_trans_N	e6mfzB3	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	e6mfzB4	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	e6mfzB2	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	PF00668	Condensation domain (Condensation)	Condensation domain	-	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	PF00550	Phosphopantetheine attachment site (PP-binding)	Phosphopantetheine attachment site	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes memb ...	A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.	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 synthase subunit A	vitamin binding amide binding modified amino acid binding binding phosphopantetheine binding small molecule binding catalytic activity ligase activity	secondary metabolite biosynthetic process biosynthetic process metabolic process cellular process secondary metabolic process antibiotic metabolic process antibiotic biosynthetic process amino acid activation peptide biosynthetic process amino acid activation for nonribosomal peptide biosynthetic process amino acid metabolic process primary metabolic process nonribosomal peptide biosynthetic process peptide metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

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	IPR020806	Polyketide synthase-like, phosphopantetheine-binding 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	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 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.