Annotations: 1ZGH

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1zgha1	All beta proteins	FMT C-terminal domain-like	FMT C-terminal domain-like	Post formyltransferase domain	Methionyl-tRNAfmet formyltransferase, C-terminal domain	(Acetivibrio thermocellus ATCC 27405 ) [TaxId: 203119 ],	SCOPe (2.08)
A	d1zgha2	Alpha and beta proteins (a/b)	Formyltransferase	Formyltransferase	Formyltransferase	Methionyl-tRNAfmet formyltransferase	(Acetivibrio thermocellus ATCC 27405 ) [TaxId: 203119 ],	SCOPe (2.08)
A	d1zgha3	Artifacts	Tags	Tags	Tags	N-terminal Tags	(Acetivibrio thermocellus ATCC 27405 ) [TaxId: 203119 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Methionyl-tRNA formyltransferase-like	8044607	4000133	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	FMT C-terminal domain-like	8044609	3000015	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Formyltransferase	8044608	3000030	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF21553	e1zghA1	A: beta barrels	X: FMT C-terminal domain-like	H: FMT C-terminal domain-related (From Topology)	T: FMT C-terminal domain-related	F: PF21553	ECOD (1.6)
A	PF00551	e1zghA2	A: a/b three-layered sandwiches	X: Formyltransferase (From Topology)	H: Formyltransferase (From Topology)	T: Formyltransferase	F: PF00551	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.170	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Formyl transferase, N-terminal domain	CATH (4.3.0)
A	3.10.25.20	Alpha Beta	Roll	Methionyl-tRNA Fmet Formyltransferase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF21553	Methionyl-tRNA formyltransferase, C-terminal domain (Formyl_trans_C_2)	Methionyl-tRNA formyltransferase, C-terminal domain	This domain is found at the C-terminal end of Methionyl-tRNA formyltransferase from Acetivibrio thermocellus and similar bacterial sequences. This domain is usually found associated with Pfam:PF00551.	Domain
A	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	Methionyl-tRNA formyltransferase	catalytic activity	biosynthetic process metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR002376	Formyl transferase, N-terminal	Domain
A	IPR036477	Formyl transferase, N-terminal domain superfamily	Homologous Superfamily
A	IPR011034	Formyl transferase-like, C-terminal domain superfamily	Homologous Superfamily
A	IPR049355	Methionyl-tRNA formyltransferase-like, C-terminal 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 R01GM133198.