2FHK

Crystal structure of formylmethanofuran: tetrahydromethanopterin formyltransferase in complex with its coenzymes

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d2fhkb1	Alpha and beta proteins (a+b)	Ferredoxin-like	Formylmethanofuran:tetrahydromethanopterin formyltransferase	Formylmethanofuran:tetrahydromethanopterin formyltransferase	Formylmethanofuran:tetrahydromethanopterin formyltransferase	(Methanopyrus kandleri ) [TaxId: 2320 ],	SCOPe (2.08)
D	d2fhkd1	Alpha and beta proteins (a+b)	Ferredoxin-like	Formylmethanofuran:tetrahydromethanopterin formyltransferase	Formylmethanofuran:tetrahydromethanopterin formyltransferase	Formylmethanofuran:tetrahydromethanopterin formyltransferase	(Methanopyrus kandleri ) [TaxId: 2320 ],	SCOPe (2.08)
A	d2fhka1	Alpha and beta proteins (a+b)	Ferredoxin-like	Formylmethanofuran:tetrahydromethanopterin formyltransferase	Formylmethanofuran:tetrahydromethanopterin formyltransferase	Formylmethanofuran:tetrahydromethanopterin formyltransferase	(Methanopyrus kandleri ) [TaxId: 2320 ],	SCOPe (2.08)
C	d2fhkc1	Alpha and beta proteins (a+b)	Ferredoxin-like	Formylmethanofuran:tetrahydromethanopterin formyltransferase	Formylmethanofuran:tetrahydromethanopterin formyltransferase	Formylmethanofuran:tetrahydromethanopterin formyltransferase	(Methanopyrus kandleri ) [TaxId: 2320 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	Formylmethanofuran:tetrahydromethanopterin formyltransferase	8035659	3001339	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Formylmethanofuran:tetrahydromethanopterin formyltransferase	8035657	3001339	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Formylmethanofuran:tetrahydromethanopterin formyltransferase	8035657	3001339	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Formylmethanofuran:tetrahydromethanopterin formyltransferase	8035659	3001339	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Formylmethanofuran:tetrahydromethanopterin formyltransferase	8035659	3001339	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Formylmethanofuran:tetrahydromethanopterin formyltransferase	8035657	3001339	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Formylmethanofuran:tetrahydromethanopterin formyltransferase	8035657	3001339	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Formylmethanofuran:tetrahydromethanopterin formyltransferase	8035659	3001339	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	FTR	e2fhkB1	A: a+b two layers	X: Alpha-beta plaits	H: Formylmethanofuran:tetrahydromethanopterin formyltransferase (From Topology)	T: Formylmethanofuran:tetrahydromethanopterin formyltransferase	F: FTR	ECOD (1.6)
B	FTR_C	e2fhkB2	A: a+b two layers	X: Alpha-beta plaits	H: Formylmethanofuran:tetrahydromethanopterin formyltransferase (From Topology)	T: Formylmethanofuran:tetrahydromethanopterin formyltransferase	F: FTR_C	ECOD (1.6)
D	FTR	e2fhkD1	A: a+b two layers	X: Alpha-beta plaits	H: Formylmethanofuran:tetrahydromethanopterin formyltransferase (From Topology)	T: Formylmethanofuran:tetrahydromethanopterin formyltransferase	F: FTR	ECOD (1.6)
D	FTR_C	e2fhkD2	A: a+b two layers	X: Alpha-beta plaits	H: Formylmethanofuran:tetrahydromethanopterin formyltransferase (From Topology)	T: Formylmethanofuran:tetrahydromethanopterin formyltransferase	F: FTR_C	ECOD (1.6)
A	FTR	e2fhkA1	A: a+b two layers	X: Alpha-beta plaits	H: Formylmethanofuran:tetrahydromethanopterin formyltransferase (From Topology)	T: Formylmethanofuran:tetrahydromethanopterin formyltransferase	F: FTR	ECOD (1.6)
A	FTR_C	e2fhkA2	A: a+b two layers	X: Alpha-beta plaits	H: Formylmethanofuran:tetrahydromethanopterin formyltransferase (From Topology)	T: Formylmethanofuran:tetrahydromethanopterin formyltransferase	F: FTR_C	ECOD (1.6)
C	FTR	e2fhkC1	A: a+b two layers	X: Alpha-beta plaits	H: Formylmethanofuran:tetrahydromethanopterin formyltransferase (From Topology)	T: Formylmethanofuran:tetrahydromethanopterin formyltransferase	F: FTR	ECOD (1.6)
C	FTR_C	e2fhkC2	A: a+b two layers	X: Alpha-beta plaits	H: Formylmethanofuran:tetrahydromethanopterin formyltransferase (From Topology)	T: Formylmethanofuran:tetrahydromethanopterin formyltransferase	F: FTR_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.30.70.520	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
D	3.30.70.520	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
A	3.30.70.520	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)
C	3.30.70.520	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01913	Formylmethanofuran-tetrahydromethanopterin formyltransferase (FTR)	Formylmethanofuran-tetrahydromethanopterin formyltransferase	This enzyme EC:2.3.1.101 is involved in archaebacteria in the formation of methane from carbon dioxide. N-terminal distal lobe of alpha+beta ferredoxin-like fold. SCOP reports fold duplication with C-terminal proximal lobe.	Domain
A, B, C, D	PF02741	FTR, proximal lobe (FTR_C)	FTR, proximal lobe	The FTR (Formylmethanofuran--tetrahydromethanopterin formyltransferase) enzyme EC:2.3.1.101 is involved in archaebacteria in the formation of methane from carbon dioxide. C-terminal proximal lobe of alpha+beta ferredoxin-like fold. SCOP reports fold ...	The FTR (Formylmethanofuran--tetrahydromethanopterin formyltransferase) enzyme EC:2.3.1.101 is involved in archaebacteria in the formation of methane from carbon dioxide. C-terminal proximal lobe of alpha+beta ferredoxin-like fold. SCOP reports fold duplication with N-terminal distal lobe.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Formylmethanofuran--tetrahydromethanopterin formyltransferase	formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity N-acyltransferase activity	cellular respiration energy derivation by oxidation of organic compounds alkane biosynthetic process methane metabolic process generation of precursor metabolites and energy hydrocarbon metabolic process alkane metabolic process biosynthetic process energy derivation by oxidation of reduced inorganic compounds methanogenesis metabolic process cellular process hydrocarbon biosynthetic process methanogenesis, from carbon dioxide cellular respiration energy derivation by oxidation of organic compounds alkane biosynthetic process methane metabolic process generation of precursor metabolites and energy hydrocarbon metabolic process alkane metabolic process biosynthetic process energy derivation by oxidation of reduced inorganic compounds methanogenesis metabolic process cellular process hydrocarbon biosynthetic process methanogenesis, from carbon dioxide anaerobic respiration small molecule metabolic process one-carbon metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR014053	Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr	Family
A, B, C, D	IPR022667	Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, N-terminal	Domain
A, B, C, D	IPR023447	Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, ferredoxin-like superfamily	Homologous Superfamily
A, B, C, D	IPR002770	Formylmethanofuran: tetrahydromethanopterin formyltransferase Ftr, C-terminal	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.