1OMS

Structure determination by MAD: E.coli Trigger Factor binding at the ribosomal exit tunnel.

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	d1omsa_	Alpha and beta proteins (a+b)	Ribosome binding domain-like	Trigger factor ribosome-binding domain	Trigger factor ribosome-binding domain	Trigger factor ribosome-binding domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1omsb_	Alpha and beta proteins (a+b)	Ribosome binding domain-like	Trigger factor ribosome-binding domain	Trigger factor ribosome-binding domain	Trigger factor ribosome-binding domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1omsc1	Alpha and beta proteins (a+b)	Ribosome binding domain-like	Trigger factor ribosome-binding domain	Trigger factor ribosome-binding domain	Trigger factor ribosome-binding domain	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
C	d1omsc2	Artifacts	Tags	Tags	Tags	N-terminal Tags	(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	Trigger factor ribosome-binding domain	8037652	3001141	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	Trigger factor ribosome-binding domain	8037652	3001141	SCOP2B (2022-06-29)
C	SCOP2 Family	Trigger factor ribosome-binding domain	8025273	4001241	SCOP2 (2022-06-29)
C	SCOP2 Superfamily	Trigger factor ribosome-binding domain	8037652	3001141	SCOP2 (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	Trigger_N	e1omsA1	A: a+b two layers	X: Glucose permease domain IIB-like	H: Trigger factor ribosome-binding domain (From Topology)	T: Trigger factor ribosome-binding domain	F: Trigger_N	ECOD (1.6)
B	Trigger_N	e1omsB1	A: a+b two layers	X: Glucose permease domain IIB-like	H: Trigger factor ribosome-binding domain (From Topology)	T: Trigger factor ribosome-binding domain	F: Trigger_N	ECOD (1.6)
C	Trigger_N	e1omsC1	A: a+b two layers	X: Glucose permease domain IIB-like	H: Trigger factor ribosome-binding domain (From Topology)	T: Trigger factor ribosome-binding domain	F: Trigger_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.70.1050	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Trigger factor ribosome-binding domain	CATH (4.3.0)
B	3.30.70.1050	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Trigger factor ribosome-binding domain	CATH (4.3.0)
C	3.30.70.1050	Alpha Beta	2-Layer Sandwich	Alpha-Beta Plaits	Trigger factor ribosome-binding domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF05697	Bacterial trigger factor protein (TF) (Trigger_N)	Bacterial trigger factor protein (TF)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	Trigger Factor	isomerase activity catalytic activity, acting on a protein peptidyl-prolyl cis-trans isomerase activity catalytic activity cis-trans isomerase activity ribonucleoprotein complex binding protein-containing complex binding binding ribosome binding protein folding chaperone identical protein binding protein binding	primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process 'de novo' cotranslational protein folding metabolic process cellular process protein metabolic process macromolecule metabolic process 'de novo' protein folding protein unfolding cell division primary metabolic process gene expression macromolecule biosynthetic process protein maturation protein folding biosynthetic process 'de novo' cotranslational protein folding metabolic process cellular process protein metabolic process macromolecule metabolic process 'de novo' protein folding protein unfolding cell division chaperone-mediated protein folding protein localization establishment of protein localization cellular localization nitrogen compound transport transport establishment of localization localization protein transport cellular macromolecule localization macromolecule localization response to stimulus response to stress response to heat response to abiotic stimulus response to temperature stimulus response to copper ion response to metal ion response to chemical stress response to copper ion stress response to metal ion	cellular anatomical structure membrane intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR046357	Peptidyl-prolyl cis-trans isomerase domain superfamily	Homologous Superfamily
A, B, C	IPR036611	Trigger factor ribosome-binding domain superfamily	Homologous Superfamily
A, B, C	IPR008881	Trigger factor, ribosome-binding, bacterial	Domain
A, B, C	IPR027304	Trigger factor/SurA domain superfamily	Homologous Superfamily
A, B, C	IPR037041	Trigger factor, C-terminal domain superfamily	Homologous Superfamily
A, B, C	IPR001179	FKBP-type peptidyl-prolyl cis-trans isomerase domain	Domain
A, B, C	IPR008880	Trigger factor, C-terminal	Domain
A, B, C	IPR005215	Trigger factor	Family

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.