3DGS

Changing the determinants of protein stability from covalent to non-covalent interactions by in-vitro evolution: a structural and energetic analysis

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	d3dgsa2	All beta proteins	N-terminal domains of the minor coat protein g3p	N-terminal domains of the minor coat protein g3p	N-terminal domains of the minor coat protein g3p	automated matches	(Enterobacteria phage fd ) [TaxId: 10864 ],	SCOPe (2.08)
A	d3dgsa1	All beta proteins	N-terminal domains of the minor coat protein g3p	N-terminal domains of the minor coat protein g3p	automated matches	automated matches	(Enterobacteria phage fd ) [TaxId: 10864 ],	SCOPe (2.08)
A	d3dgsa3	Artifacts	Tags	Tags	Tags	C-terminal Tags	(Enterobacteria phage fd ) [TaxId: 10864 ],	SCOPe (2.08)
B	d3dgsb2	All beta proteins	N-terminal domains of the minor coat protein g3p	N-terminal domains of the minor coat protein g3p	N-terminal domains of the minor coat protein g3p	automated matches	(Enterobacteria phage fd ) [TaxId: 10864 ],	SCOPe (2.08)
B	d3dgsb1	All beta proteins	N-terminal domains of the minor coat protein g3p	N-terminal domains of the minor coat protein g3p	automated matches	automated matches	(Enterobacteria phage fd ) [TaxId: 10864 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	N-terminal domains of the minor coat protein g3p	8041745	3000411	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	N-terminal domains of the minor coat protein g3p	8041744	3000411	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	N-terminal domains of the minor coat protein g3p	8041744	3000411	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	N-terminal domains of the minor coat protein g3p	8041745	3000411	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	PF05357	e3dgsA1	A: beta meanders	X: N-terminal domains of the minor coat protein g3p (From Topology)	H: N-terminal domains of the minor coat protein g3p (From Topology)	T: N-terminal domains of the minor coat protein g3p	F: PF05357	ECOD (1.6)
B	PF05357	e3dgsB1	A: beta meanders	X: N-terminal domains of the minor coat protein g3p (From Topology)	H: N-terminal domains of the minor coat protein g3p (From Topology)	T: N-terminal domains of the minor coat protein g3p	F: PF05357	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.30.27.10	Mainly Beta	Roll	Phage FD Coat Protein, Membrane penetration domain	Phage FD Coat Protein,Membrane penetration domain	CATH (4.3.0)
A	3.90.450.1	Alpha Beta	Alpha-Beta Complex	Minor Coat Protein	domain 2	CATH (4.3.0)
B	2.30.27.10	Mainly Beta	Roll	Phage FD Coat Protein, Membrane penetration domain	Phage FD Coat Protein,Membrane penetration domain	CATH (4.3.0)
B	3.90.450.1	Alpha Beta	Alpha-Beta Complex	Minor Coat Protein	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF05357	Phage Coat Protein A (Phage_Coat_A)	Phage Coat Protein A	Infection of Escherichia coli by filamentous bacteriophages is mediated by the minor phage coat protein A and involves two distinct cellular receptors, the F' pilus and the periplasmic protein TolA. These two receptors are contacted in a sequential ...	Infection of Escherichia coli by filamentous bacteriophages is mediated by the minor phage coat protein A and involves two distinct cellular receptors, the F' pilus and the periplasmic protein TolA. These two receptors are contacted in a sequential manner, such that binding of TolA by the extreme N-terminal domain is conditional on a primary interaction of the second coat protein A domain with the F' pilus [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Coat protein A	-	virion attachment to host cell biological process involved in interspecies interaction between organisms receptor-mediated virion attachment to host cell adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host adhesion receptor-mediated virion attachment to host cell biological process involved in interaction with host biological process involved in symbiotic interaction exit from host cell non-lytic viral release viral extrusion viral release from host cell virion attachment to host cell biological process involved in interspecies interaction between organisms receptor-mediated virion attachment to host cell adhesion of symbiont to host cell viral process viral life cycle adhesion of symbiont to host adhesion receptor-mediated virion attachment to host cell biological process involved in interaction with host biological process involved in symbiotic interaction exit from host cell non-lytic viral release viral extrusion viral release from host cell entry receptor-mediated virion attachment to host cell virion attachment to host cell pilus symbiont entry into host cell symbiont entry into host	viral capsid virion component host cellular component host cell part host cell membrane cellular anatomical entity membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036200	Attachment protein G3P, N-terminal domain superfamily	Homologous Superfamily
A, B	IPR013834	Bacteriophage, G3P, N2-domain superfamily	Homologous Superfamily
A, B	IPR008021	Attachment protein G3P, N-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 R01GM133198.