1BSZ

PEPTIDE DEFORMYLASE AS FE2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1bsza_	Alpha and beta proteins (a+b)	Peptide deformylase	Peptide deformylase	Peptide deformylase	Peptide deformylase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
B	d1bszb_	Alpha and beta proteins (a+b)	Peptide deformylase	Peptide deformylase	Peptide deformylase	Peptide deformylase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)
C	d1bszc_	Alpha and beta proteins (a+b)	Peptide deformylase	Peptide deformylase	Peptide deformylase	Peptide deformylase	(Escherichia coli K-12 ) [TaxId: 83333 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Peptide deformylase	8033706	3001229	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Peptide deformylase	8033706	3001229	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Peptide deformylase	8033706	3001229	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	PF01327	e1bszA1	A: a+b complex topology	X: Peptide deformylase (From Topology)	H: Peptide deformylase (From Topology)	T: Peptide deformylase	F: PF01327	ECOD (1.6)
B	PF01327	e1bszB1	A: a+b complex topology	X: Peptide deformylase (From Topology)	H: Peptide deformylase (From Topology)	T: Peptide deformylase	F: PF01327	ECOD (1.6)
C	PF01327	e1bszC1	A: a+b complex topology	X: Peptide deformylase (From Topology)	H: Peptide deformylase (From Topology)	T: Peptide deformylase	F: PF01327	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.90.45.10	Alpha Beta	Alpha-Beta Complex	Peptide Deformylase	Peptide deformylase	CATH (4.3.0)
B	3.90.45.10	Alpha Beta	Alpha-Beta Complex	Peptide Deformylase	Peptide deformylase	CATH (4.3.0)
C	3.90.45.10	Alpha Beta	Alpha-Beta Complex	Peptide Deformylase	Peptide deformylase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF01327	Polypeptide deformylase (Pep_deformylase)	Polypeptide deformylase	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	PROTEIN (PEPTIDE DEFORMYLASE)	peptide deformylase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding zinc ion binding peptide deformylase activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides hydrolase activity catalytic activity hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds cation binding transition metal ion binding iron ion binding ion binding binding ferrous iron binding metal ion binding small molecule binding zinc ion binding ribonucleoprotein complex binding protein-containing complex binding ribosome binding	organic substance metabolic process organonitrogen compound metabolic process macromolecule modification metabolic process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process co-translational protein modification cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process translation gene expression organic substance metabolic process organonitrogen compound metabolic process macromolecule modification metabolic process primary metabolic process protein metabolic process macromolecule metabolic process protein modification process co-translational protein modification cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process translation gene expression macromolecule biosynthetic process biosynthetic process organic substance biosynthetic process cellular process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR023635	Peptide deformylase	Family
A, B, C	IPR036821	Peptide deformylase superfamily	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
C	peptide deformylase M-CSA #98	In prokaryotes, proteins are synthesised with an N-terminal formylmethionine which is removed by peptide deformylase. Eukaryotes do not use this enzyme, so it represents a potential drug target for the treatment of bacterial infections.	Defined by 7 residues: GLY:C-45 [auth C-1045]GLN:C-50 [auth C-1050]CYS:C-90 [auth C-1090]LEU:C-91 [auth C-1091]HIS:C-132 [auth C-1132]GLU:C-133 [auth C-1133]HIS:C-136 [auth C-1136] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 3.5.1.31 (PDB Primary Data) Search M-CSA Motif + EC 3.5.1.31

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.