1CM5

CRYSTAL STRUCTURE OF C418A,C419A MUTANT OF PFL FROM E.COLI

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)
A	d1cm5a_	Alpha and beta proteins (a/b)	PFL-like glycyl radical enzymes	PFL-like glycyl radical enzymes	PFL-like	Pyruvate formate-lyase, PFL	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1cm5b_	Alpha and beta proteins (a/b)	PFL-like glycyl radical enzymes	PFL-like glycyl radical enzymes	PFL-like	Pyruvate formate-lyase, PFL	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	PFL-like glycyl radical enzymes	8042340	3001069	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	PFL-like glycyl radical enzymes	8042340	3001069	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)
A	PFL-like	e1cm5A2	A: a/b barrels	X: Ten stranded beta/alpha barrel (From Topology)	H: Ten stranded beta/alpha barrel (From Topology)	T: Ten stranded beta/alpha barrel	F: PFL-like	ECOD (1.6)
A	PFL-like	e1cm5A1	A: extended segments	X: Glycyl radical domain (From Topology)	H: Glycyl radical domain (From Topology)	T: Glycyl radical domain	F: PFL-like	ECOD (1.6)
B	PFL-like	e1cm5B2	A: a/b barrels	X: Ten stranded beta/alpha barrel (From Topology)	H: Ten stranded beta/alpha barrel (From Topology)	T: Ten stranded beta/alpha barrel	F: PFL-like	ECOD (1.6)
B	PFL-like	e1cm5B1	A: extended segments	X: Glycyl radical domain (From Topology)	H: Glycyl radical domain (From Topology)	T: Glycyl radical domain	F: PFL-like	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.20.70.20	Alpha Beta	Alpha-Beta Barrel	Anaerobic Ribonucleotide-triphosphate Reductase Large Chain		CATH (4.3.0)
B	3.20.70.20	Alpha Beta	Alpha-Beta Barrel	Anaerobic Ribonucleotide-triphosphate Reductase Large Chain		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01228	Glycine radical (Gly_radical)	Glycine radical	-	Domain
A, B	PF02901	Pyruvate formate lyase-like (PFL-like)	Pyruvate formate lyase-like	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROTEIN (PYRUVATE FORMATE-LYASE)	acetyltransferase activity acyltransferase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity C-acyltransferase activity C-acetyltransferase activity formate C-acetyltransferase activity	glycolytic fermentation energy derivation by oxidation of organic compounds cellular metabolic process metabolic process cellular process generation of precursor metabolites and energy glycolytic fermentation via PFL pathway fermentation monosaccharide metabolic process carbohydrate metabolic process hexose metabolic process small molecule metabolic process primary metabolic process glucose metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR004184	Pyruvate formate lyase domain	Domain
A, B	IPR001150	Glycine radical domain	Domain
A, B	IPR005949	Formate acetyltransferase	Family
A, B	IPR050244	Autonomous Glycyl Radical Cofactor	Family
A, B	IPR019777	Formate C-acetyltransferase glycine radical, conserved site	Conserved Site

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.