4NV1

Crystal structure of a 4-N formyltransferase from Francisella tularensis

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 [auth C]	PRK07579	e4nv1C2	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
A [auth C]	Formyl_trans_N	e4nv1C1	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
B [auth D]	PRK07579	e4nv1D2	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
B [auth D]	Formyl_trans_N	e4nv1D1	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
C [auth E]	PRK07579	e4nv1E1	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
C [auth E]	Formyl_trans_N	e4nv1E2	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
D [auth F]	PRK07579	e4nv1F2	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
D [auth F]	Formyl_trans_N	e4nv1F1	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
E [auth B]	PRK07579	e4nv1B1	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
E [auth B]	Formyl_trans_N	e4nv1B2	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
F [auth A]	PRK07579	e4nv1A2	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
F [auth A]	Formyl_trans_N	e4nv1A1	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
G	PRK07579	e4nv1G2	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
G	Formyl_trans_N	e4nv1G1	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)
H	PRK07579	e4nv1H2	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PRK07579	ECOD (1.6)
H	Formyl_trans_N	e4nv1H1	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: Formyl_trans_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A [auth C]	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)
B [auth D]	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)
C [auth E]	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)
D [auth F]	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)
E [auth B]	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)
F [auth A]	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)
G	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)
H	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], F [auth A], G, H	PF18216	N-formyltransferase dimerization C-terminal domain (N_formyltrans_C)	N-formyltransferase dimerization C-terminal domain	This is the C-terminal domain of N-formyltransferase found in Francisella tularensis. N-formylated sugars are observed on O-antigens of pathogenic Gram-negative bacteria. This C-terminal domain is responsible for dimerization. In particular, the beta ...	This is the C-terminal domain of N-formyltransferase found in Francisella tularensis. N-formylated sugars are observed on O-antigens of pathogenic Gram-negative bacteria. This C-terminal domain is responsible for dimerization. In particular, the beta hairpin motif present in the domain helps create a subunit-subunit interface. The dimeric interface is characterized by a hydrophobic patch formed by Ile 195, Leu 197, Val 201, Met 203, Ile 207, Phe 223, Val 231, Val 233, Leu 235, and Leu 237 from both monomers [1].	Domain
A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], F [auth A], G, H	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 [auth C], B [auth D], C [auth E], D [auth F], E [auth B], A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], F [auth A], G, H	Formyltransferase	transferase activity catalytic activity	biosynthetic process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], F [auth A], G, H	IPR001555	Phosphoribosylglycinamide formyltransferase, active site	Active Site
A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], F [auth A], G, H	IPR040660	N-formyltransferase dimerization C-terminal domain	Domain
A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], F [auth A], G, H	IPR002376	Formyl transferase, N-terminal	Domain
A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], A [auth C], B [auth D], C [auth E], D [auth F], E [auth B], F [auth A], G, H	IPR036477	Formyl transferase, N-terminal domain superfamily	Homologous Superfamily

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.