1BXY

CRYSTAL STRUCTURE OF RIBOSOMAL PROTEIN L30 FROM THERMUS THERMOPHILUS AT 1.9 A RESOLUTION: CONFORMATIONAL FLEXIBILITY OF THE MOLECULE.

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	d1bxya_	Alpha and beta proteins (a+b)	Ribosomal protein L30p/L7e	Ribosomal protein L30p/L7e	Ribosomal protein L30p/L7e	Prokaryotic ribosomal protein L30	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)
B	d1bxyb_	Alpha and beta proteins (a+b)	Ribosomal protein L30p/L7e	Ribosomal protein L30p/L7e	Ribosomal protein L30p/L7e	Prokaryotic ribosomal protein L30	(Thermus thermophilus ) [TaxId: 274 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Ribosomal protein L30p/L7e	8023319	4001360	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Ribosomal protein L30p/L7e	8035699	3001378	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	Ribosomal protein L30p/L7e	8035699	3001378	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	Ribosomal_L30	e1bxyA1	A: a+b two layers	X: Ribosomal protein L30p/L7e (From Topology)	H: Ribosomal protein L30p/L7e (From Topology)	T: Ribosomal protein L30p/L7e	F: Ribosomal_L30	ECOD (1.6)
B	Ribosomal_L30	e1bxyB1	A: a+b two layers	X: Ribosomal protein L30p/L7e (From Topology)	H: Ribosomal protein L30p/L7e (From Topology)	T: Ribosomal protein L30p/L7e	F: Ribosomal_L30	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.1390.20	Alpha Beta	2-Layer Sandwich	Ribosomal Protein L30	Chain: A,	CATH (4.3.0)
B	3.30.1390.20	Alpha Beta	2-Layer Sandwich	Ribosomal Protein L30	Chain: A,	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00327	Ribosomal protein L30p/L7e (Ribosomal_L30)	Ribosomal protein L30p/L7e	This family includes prokaryotic L30 and eukaryotic L7.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	PROTEIN (RIBOSOMAL PROTEIN L30)	structural molecule activity structural constituent of ribosome	biosynthetic process metabolic process cellular process primary metabolic process protein metabolic process macromolecule metabolic process translation gene expression macromolecule biosynthetic process	protein-containing complex intracellular anatomical structure intracellular membraneless organelle intracellular organelle ribosomal subunit cytosolic large ribosomal subunit cellular anatomical structure cytosolic ribosome organelle ribonucleoprotein complex membraneless organelle ribosome cytoplasm cytosol protein-containing complex intracellular anatomical structure intracellular membraneless organelle intracellular organelle ribosomal subunit cytosolic large ribosomal subunit cellular anatomical structure cytosolic ribosome organelle ribonucleoprotein complex membraneless organelle ribosome cytoplasm cytosol large ribosomal subunit

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR036919	Large ribosomal subunit protein uL30, ferredoxin-like fold domain superfamily	Homologous Superfamily
A, B	IPR005996	Large ribosomal subunit protein uL30, bacterial-type	Family
A, B	IPR016082	Large ribosomal subunit protein uL30-like, ferredoxin-like fold domain	Domain
A, B	IPR018038	Large ribosomal subunit protein uL30, conserved site	Conserved Site

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.