1SZZ

Crystal structure of peptide deformylase from Leptospira Interrogans complexed with inhibitor actinonin

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
E	SCOP2B Superfamily	Peptide deformylase	8044284	3001229	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Peptide deformylase	8044284	3001229	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Peptide deformylase	8044284	3001229	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	Peptide deformylase	8044284	3001229	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	Peptide deformylase	8044284	3001229	SCOP2B (2022-06-29)
F	SCOP2B Superfamily	Peptide deformylase	8044284	3001229	SCOP2B (2022-06-29)
G	SCOP2B Superfamily	Peptide deformylase	8044284	3001229	SCOP2B (2022-06-29)
H	SCOP2B Superfamily	Peptide deformylase	8044284	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)
E	PF01327	e1szzE1	A: a+b complex topology	X: Peptide deformylase (From Topology)	H: Peptide deformylase (From Topology)	T: Peptide deformylase	F: PF01327	ECOD (1.6)
A	PF01327	e1szzA1	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	e1szzB1	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	e1szzC1	A: a+b complex topology	X: Peptide deformylase (From Topology)	H: Peptide deformylase (From Topology)	T: Peptide deformylase	F: PF01327	ECOD (1.6)
D	PF01327	e1szzD1	A: a+b complex topology	X: Peptide deformylase (From Topology)	H: Peptide deformylase (From Topology)	T: Peptide deformylase	F: PF01327	ECOD (1.6)
F	PF01327	e1szzF1	A: a+b complex topology	X: Peptide deformylase (From Topology)	H: Peptide deformylase (From Topology)	T: Peptide deformylase	F: PF01327	ECOD (1.6)
G	PF01327	e1szzG1	A: a+b complex topology	X: Peptide deformylase (From Topology)	H: Peptide deformylase (From Topology)	T: Peptide deformylase	F: PF01327	ECOD (1.6)
H	PF01327	e1szzH1	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)
E	3.90.45.10	Alpha Beta	Alpha-Beta Complex	Peptide Deformylase	Peptide deformylase	CATH (4.3.0)
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)
D	3.90.45.10	Alpha Beta	Alpha-Beta Complex	Peptide Deformylase	Peptide deformylase	CATH (4.3.0)
F	3.90.45.10	Alpha Beta	Alpha-Beta Complex	Peptide Deformylase	Peptide deformylase	CATH (4.3.0)
G	3.90.45.10	Alpha Beta	Alpha-Beta Complex	Peptide Deformylase	Peptide deformylase	CATH (4.3.0)
H	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, D, E A, B, C, D, E, F, G, H	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, D, E A, B, C, D, E, F, G, H	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 ion binding binding metal ion binding small molecule 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	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR023635	Peptide deformylase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036821	Peptide deformylase superfamily	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.