2JYN | pdb_00002jyn

A novel solution NMR structure of protein yst0336 from Saccharomyces cerevisiae. Northeast Structural Genomics Consortium target YT51/Ontario Centre for Structural Proteomics target yst0336

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)
A	SCOP2 Family	Yst0336-like	8046294	4005006	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	His-Me finger endonucleases	8093363	3001893	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	Polysacc_synt_4	e2jynA1	A: alpha arrays	X: Yst0336-like (From Topology)	H: Yst0336-like (From Topology)	T: Yst0336-like	F: Polysacc_synt_4	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.3560.10	Mainly Alpha	Orthogonal Bundle	yst0336 like fold	yst0336 like domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF04669	PBDC1 protein (PBDC1)	PBDC1 protein	This entry includes PBDC1 protein from mammals and its homologues from fungi. PBDC1 homolog from S. cerevisiae also known as Ypl225w (Chp1, Chaperone 1 for eEF1A) functions as a co-translational chaperone by forming dual interactions with the eEF1A G ...	This entry includes PBDC1 protein from mammals and its homologues from fungi. PBDC1 homolog from S. cerevisiae also known as Ypl225w (Chp1, Chaperone 1 for eEF1A) functions as a co-translational chaperone by forming dual interactions with the eEF1A G domain nascent chain and the UBA domain of ribosome-bound nascent polypeptide-associated complex [1]. This protein primes the eEF1A nascent chains for binding to GTP as part of a folding mechanism which is tightly coupled to chaperone recycling [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	UPF0368 protein YPL225W	protein folding chaperone protein-containing complex binding binding nascent polypeptide-associated complex binding protein binding misfolded protein binding translation elongation factor binding ribonucleoprotein complex binding ribosome 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	cellular anatomical structure intracellular anatomical structure cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR008476	Protein PBDC1, metazoa/fungi	Family
A	IPR021148	Polysaccharide biosynthesis domain	Domain
A	IPR023139	PBDC1-like domain superfamily	Homologous Superfamily

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.