1SBQ

Crystal Structure of methenyltetrahydrofolate synthetase from Mycoplasma pneumoniae at 2.2 resolution

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	d1sbqa_	Alpha and beta proteins (a/b)	NagB/RpiA/CoA transferase-like	NagB/RpiA/CoA transferase-like	Methenyltetrahydrofolate synthetase	5,10-methenyltetrahydrofolate synthetase homolog MPN348	(Mycoplasmoides pneumoniae ) [TaxId: 2104 ],	SCOPe (2.08)
B	d1sbqb_	Alpha and beta proteins (a/b)	NagB/RpiA/CoA transferase-like	NagB/RpiA/CoA transferase-like	Methenyltetrahydrofolate synthetase	5,10-methenyltetrahydrofolate synthetase homolog MPN348	(Mycoplasmoides pneumoniae ) [TaxId: 2104 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Methenyltetrahydrofolate synthetase-like	8026952	4002105	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	NagB/RpiA/CoA transferase-like	8039331	3000693	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	NagB/RpiA/CoA transferase-like	8039331	3000693	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	5-FTHF_cyc-lig	e1sbqA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: 5-FTHF_cyc-lig	ECOD (1.6)
B	5-FTHF_cyc-lig	e1sbqB1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: 5-FTHF_cyc-lig	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.10420	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NagB/RpiA/CoA transferase-like	CATH (4.3.0)
B	3.40.50.10420	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NagB/RpiA/CoA transferase-like	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01812	5-formyltetrahydrofolate cyclo-ligase family (5-FTHF_cyc-lig)	5-formyltetrahydrofolate cyclo-ligase family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	5,10-Methenyltetrahydrofolate synthetase homolog	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding catalytic activity cyclo-ligase activity ligase activity, forming carbon-nitrogen bonds 5-formyltetrahydrofolate cyclo-ligase activity ligase activity cation binding metal ion binding	-	intracellular anatomical structure cytoplasm cellular anatomical entity

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR024185	5-formyltetrahydrofolate cyclo-ligase-like domain superfamily	Homologous Superfamily
A, B	IPR037171	NagB/RpiA transferase-like	Homologous Superfamily
A, B	IPR002698	5-formyltetrahydrofolate cyclo-ligase	Family

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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.