5O96

Structure of the putative methyltransferase Lpg2936 from Legionella pneumophila in complex with the bound cofactor SAM

External Resource: Annotation

Domain Annotation: SCOP/SCOPe 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	d5o96a1	All beta proteins	PUA domain-like	PUA domain-like	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
A	d5o96a2	Alpha and beta proteins (a/b)	alpha/beta knot	alpha/beta knot	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
B	d5o96b1	All beta proteins	PUA domain-like	PUA domain-like	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
B	d5o96b2	Alpha and beta proteins (a/b)	alpha/beta knot	alpha/beta knot	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
C	d5o96c1	All beta proteins	PUA domain-like	PUA domain-like	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
C	d5o96c2	Alpha and beta proteins (a/b)	alpha/beta knot	alpha/beta knot	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
D	d5o96d1	All beta proteins	PUA domain-like	PUA domain-like	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
D	d5o96d2	Alpha and beta proteins (a/b)	alpha/beta knot	alpha/beta knot	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
F	d5o96f1	All beta proteins	PUA domain-like	PUA domain-like	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
F	d5o96f2	Alpha and beta proteins (a/b)	alpha/beta knot	alpha/beta knot	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
G	d5o96g1	All beta proteins	PUA domain-like	PUA domain-like	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
G	d5o96g2	Alpha and beta proteins (a/b)	alpha/beta knot	alpha/beta knot	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
H	d5o96h1	All beta proteins	PUA domain-like	PUA domain-like	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
H	d5o96h2	Alpha and beta proteins (a/b)	alpha/beta knot	alpha/beta knot	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
E	d5o96e1	All beta proteins	PUA domain-like	PUA domain-like	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)
E	d5o96e2	Alpha and beta proteins (a/b)	alpha/beta knot	alpha/beta knot	automated matches	automated matches	(Legionella pneumophila ) [TaxId: 446 ],	SCOPe (2.08)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF20260	e5o96A2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PUA domain	F: PF20260	ECOD (1.6)
A	PF04452	e5o96A1	A: a/b three-layered sandwiches	X: alpha/beta knot (From Topology)	H: alpha/beta knot (From Topology)	T: alpha/beta knot	F: PF04452	ECOD (1.6)
B	PF20260	e5o96B2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PUA domain	F: PF20260	ECOD (1.6)
B	PF04452	e5o96B1	A: a/b three-layered sandwiches	X: alpha/beta knot (From Topology)	H: alpha/beta knot (From Topology)	T: alpha/beta knot	F: PF04452	ECOD (1.6)
C	PF20260	e5o96C2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PUA domain	F: PF20260	ECOD (1.6)
C	PF04452	e5o96C1	A: a/b three-layered sandwiches	X: alpha/beta knot (From Topology)	H: alpha/beta knot (From Topology)	T: alpha/beta knot	F: PF04452	ECOD (1.6)
D	PF20260	e5o96D2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PUA domain	F: PF20260	ECOD (1.6)
D	PF04452	e5o96D1	A: a/b three-layered sandwiches	X: alpha/beta knot (From Topology)	H: alpha/beta knot (From Topology)	T: alpha/beta knot	F: PF04452	ECOD (1.6)
F	PF20260	e5o96F1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PUA domain	F: PF20260	ECOD (1.6)
F	PF04452	e5o96F2	A: a/b three-layered sandwiches	X: alpha/beta knot (From Topology)	H: alpha/beta knot (From Topology)	T: alpha/beta knot	F: PF04452	ECOD (1.6)
G	PF20260	e5o96G2	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PUA domain	F: PF20260	ECOD (1.6)
G	PF04452	e5o96G1	A: a/b three-layered sandwiches	X: alpha/beta knot (From Topology)	H: alpha/beta knot (From Topology)	T: alpha/beta knot	F: PF04452	ECOD (1.6)
H	PF20260	e5o96H1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PUA domain	F: PF20260	ECOD (1.6)
H	PF04452	e5o96H2	A: a/b three-layered sandwiches	X: alpha/beta knot (From Topology)	H: alpha/beta knot (From Topology)	T: alpha/beta knot	F: PF04452	ECOD (1.6)
E	PF20260	e5o96E1	A: beta barrels	X: cradle loop barrel	H: RIFT-related	T: PUA domain	F: PF20260	ECOD (1.6)
E	PF04452	e5o96E2	A: a/b three-layered sandwiches	X: alpha/beta knot (From Topology)	H: alpha/beta knot (From Topology)	T: alpha/beta knot	F: PF04452	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.40.240.20	Mainly Beta	Beta Barrel	Ribosomal Protein L25	Chain P	CATH (4.3.0)
A	3.40.1280.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha/beta knot	SPOUT methyltransferase, trefoil knot domain	CATH (4.3.0)
B	2.40.240.20	Mainly Beta	Beta Barrel	Ribosomal Protein L25	Chain P	CATH (4.3.0)
B	3.40.1280.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha/beta knot	SPOUT methyltransferase, trefoil knot domain	CATH (4.3.0)
C	2.40.240.20	Mainly Beta	Beta Barrel	Ribosomal Protein L25	Chain P	CATH (4.3.0)
C	3.40.1280.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha/beta knot	SPOUT methyltransferase, trefoil knot domain	CATH (4.3.0)
D	2.40.240.20	Mainly Beta	Beta Barrel	Ribosomal Protein L25	Chain P	CATH (4.3.0)
D	3.40.1280.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha/beta knot	SPOUT methyltransferase, trefoil knot domain	CATH (4.3.0)
F	2.40.240.20	Mainly Beta	Beta Barrel	Ribosomal Protein L25	Chain P	CATH (4.3.0)
F	3.40.1280.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha/beta knot	SPOUT methyltransferase, trefoil knot domain	CATH (4.3.0)
G	2.40.240.20	Mainly Beta	Beta Barrel	Ribosomal Protein L25	Chain P	CATH (4.3.0)
G	3.40.1280.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha/beta knot	SPOUT methyltransferase, trefoil knot domain	CATH (4.3.0)
H	2.40.240.20	Mainly Beta	Beta Barrel	Ribosomal Protein L25	Chain P	CATH (4.3.0)
H	3.40.1280.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha/beta knot	SPOUT methyltransferase, trefoil knot domain	CATH (4.3.0)
E	2.40.240.20	Mainly Beta	Beta Barrel	Ribosomal Protein L25	Chain P	CATH (4.3.0)
E	3.40.1280.10	Alpha Beta	3-Layer(aba) Sandwich	Alpha/beta knot	SPOUT methyltransferase, trefoil knot domain	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	PF20260	RNA methyltransferase PUA domain (PUA_4)	RNA methyltransferase PUA domain	RNA methyltransferases modify nucleotides during ribosomal RNA maturation in a site-specific manner. The Escherichia coli member is specific for U1498 methylation [1][2].	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	PF04452	RNA methyltransferase domain (Methyltrans_RNA)	RNA methyltransferase domain	RNA methyltransferases modify nucleotides during ribosomal RNA maturation in a site-specific manner. The Escherichia coli member is specific for U1498 methylation [1][2].	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	Ribosomal RNA small subunit methyltransferase E	transferase activity, transferring one-carbon groups transferase activity methyltransferase activity catalytic activity	methylation metabolic process ribonucleoprotein complex biogenesis cellular biosynthetic process RNA metabolic process rRNA processing nucleobase-containing compound metabolic process cellular component biogenesis ribosome biogenesis organic substance metabolic process organic substance biosynthetic process cellular component organization or biogenesis RNA processing rRNA metabolic process methylation metabolic process ribonucleoprotein complex biogenesis cellular biosynthetic process RNA metabolic process rRNA processing nucleobase-containing compound metabolic process cellular component biogenesis ribosome biogenesis organic substance metabolic process organic substance biosynthetic process cellular component organization or biogenesis RNA processing rRNA metabolic process cellular metabolic process primary metabolic process gene expression macromolecule biosynthetic process nucleic acid metabolic process organic cyclic compound metabolic process biosynthetic process ncRNA metabolic process nucleic acid catabolic process cellular process macromolecule metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR015947	PUA-like superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR046886	Ribosomal RNA small subunit methyltransferase E, methyltransferase domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR006700	Ribosomal RNA small subunit methyltransferase E	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR029026	tRNA (guanine-N1-)-methyltransferase, N-terminal	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR029028	Alpha/beta knot methyltransferases	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR046887	Ribosomal RNA small subunit methyltransferase E, PUA-like domain	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.