4APB

Crystal structure of Mycobacterium tuberculosis fumarase (Rv1098c) S318C in complex with fumarate

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)
C	d4apbc_	All alpha proteins	L-aspartase-like	L-aspartase-like	automated matches	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)
A	d4apba_	All alpha proteins	L-aspartase-like	L-aspartase-like	automated matches	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)
B	d4apbb_	All alpha proteins	L-aspartase-like	L-aspartase-like	automated matches	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)
D	d4apbd_	All alpha proteins	L-aspartase-like	L-aspartase-like	automated matches	automated matches	(Mycobacterium tuberculosis H37Rv ) [TaxId: 83332 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
C	SCOP2B Superfamily	L-aspartase-like	8072365	3001572	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	L-aspartase-like	8072365	3001572	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	L-aspartase-like	8072365	3001572	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	L-aspartase-like	8072365	3001572	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)
C	Lyase_1_N	e4apbC9	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
C	FumaraseC_C	e4apbC7	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: FumaraseC_C	ECOD (1.6)
C	Lyase_1_C	e4apbC8	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)
A	Lyase_1_N	e4apbA9	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
A	FumaraseC_C	e4apbA7	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: FumaraseC_C	ECOD (1.6)
A	Lyase_1_C	e4apbA8	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)
B	Lyase_1_N	e4apbB9	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
B	FumaraseC_C	e4apbB7	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: FumaraseC_C	ECOD (1.6)
B	Lyase_1_C	e4apbB8	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)
D	Lyase_1_N	e4apbD9	A: alpha arrays	X: L-aspartase N-terminal domain-like (From Topology)	H: L-aspartase N-terminal domain-like (From Topology)	T: L-aspartase N-terminal domain-like	F: Lyase_1_N	ECOD (1.6)
D	FumaraseC_C	e4apbD7	A: alpha arrays	X: L-aspartase C-terminal domain-like (From Homology)	H: L-aspartase C-terminal domain-like	T: L-aspartase C-terminal domain-like	F: FumaraseC_C	ECOD (1.6)
D	Lyase_1_C	e4apbD8	A: alpha arrays	X: L-aspartase middle domain-like	H: L-aspartase middle domain-like (From Topology)	T: L-aspartase middle domain-like	F: Lyase_1_C	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
C	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
C	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
C	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)
A	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
A	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
A	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)
B	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
B	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
B	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)
D	1.10.275.10	Mainly Alpha	Orthogonal Bundle	Fumarase C	Chain B, domain 1	CATH (4.3.0)
D	1.20.200.10	Mainly Alpha	Up-down Bundle	Fumarase C	Chain A, domain 2	CATH (4.3.0)
D	1.10.40.30	Mainly Alpha	Orthogonal Bundle	Ribonucleotide Reductase Protein R1	domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00206	Lyase (Lyase_1)	Lyase	-	Domain
A, B, C, D	PF10415	Fumarase C C-terminus (FumaraseC_C)	Fumarase C C-terminus	Fumarase C catalyses the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The ...	Fumarase C catalyses the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit [1]. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	FUMARATE HYDRATASE CLASS II	hydro-lyase activity lyase activity catalytic activity fumarate hydratase activity carbon-oxygen lyase activity	aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds metabolic process cellular process primary metabolic process generation of precursor metabolites and energy oxoacid metabolic process dicarboxylic acid metabolic process carboxylic acid metabolic process small molecule metabolic process fumarate metabolic process organic acid metabolic process	cellular anatomical structure extracellular region intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane external encapsulating structure cell wall peptidoglycan-based cell wall

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR000362	Fumarate lyase family	Family
A, B, C, D	IPR022761	Fumarate lyase, N-terminal	Domain
A, B, C, D	IPR024083	Fumarase/histidase, N-terminal	Homologous Superfamily
A, B, C, D	IPR005677	Fumarate hydratase, class II	Family
A, B, C, D	IPR008948	L-Aspartase-like	Homologous Superfamily
A, B, C, D	IPR018951	Fumarase C, C-terminal	Domain
A, B, C, D	IPR020557	Fumarate lyase, 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.