3CSM

STRUCTURE OF YEAST CHORISMATE MUTASE WITH BOUND TRP AND AN ENDOOXABICYCLIC INHIBITOR

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Structure Motif: Primary M-CSA Annotation

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d3csma_	All alpha proteins	Chorismate mutase II	Chorismate mutase II	Allosteric chorismate mutase	Allosteric chorismate mutase	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
B	d3csmb_	All alpha proteins	Chorismate mutase II	Chorismate mutase II	Allosteric chorismate mutase	Allosteric chorismate mutase	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	chorismate mutase ii	8038920	3001645	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	chorismate mutase ii	8038920	3001645	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	PF01817	e3csmA1	A: alpha bundles	X: Chorismate mutase II (From Topology)	H: Chorismate mutase II (From Topology)	T: Chorismate mutase II	F: PF01817	ECOD (1.6)
B	PF01817	e3csmB1	A: alpha bundles	X: Chorismate mutase II (From Topology)	H: Chorismate mutase II (From Topology)	T: Chorismate mutase II	F: PF01817	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.10.590.10	Mainly Alpha	Orthogonal Bundle	Chorismate Mutase, subunit A	Chorismate mutase, AroQ class superfamily, eukaryotic	CATH (4.3.0)
B	1.10.590.10	Mainly Alpha	Orthogonal Bundle	Chorismate Mutase, subunit A	Chorismate mutase, AroQ class superfamily, eukaryotic	CATH (4.3.0)

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	CHORISMATE MUTASE	cation binding organic acid binding binding ion binding organic cyclic compound binding L-tyrosine binding anion binding amino acid binding carboxylic acid binding small molecule binding isomerase activity chorismate mutase activity catalytic activity intramolecular transferase activity cation binding organic acid binding binding ion binding organic cyclic compound binding L-tyrosine binding anion binding amino acid binding carboxylic acid binding small molecule binding isomerase activity chorismate mutase activity catalytic activity intramolecular transferase activity tryptophan binding heterocyclic compound binding	oxoacid metabolic process cellular biosynthetic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process tyrosine metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process organonitrogen compound metabolic process oxoacid metabolic process cellular biosynthetic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process alpha-amino acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process organic substance biosynthetic process small molecule metabolic process tyrosine metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process organonitrogen compound metabolic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-amino acid metabolic process aromatic amino acid family biosynthetic process, prephenate pathway organic cyclic compound metabolic process proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process organic cyclic compound biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process erythrose 4-phosphate/phosphoenolpyruvate family amino acid biosynthetic process tyrosine biosynthetic process alpha-amino acid biosynthetic process L-phenylalanine biosynthetic process L-phenylalanine metabolic process dicarboxylic acid metabolic process chorismate metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity membrane-bounded organelle intracellular organelle organelle nucleus intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR008238	Chorismate mutase, AroQ class, eukaryotic type	Family
A, B	IPR036263	Chorismate mutase type II superfamily	Homologous Superfamily
A, B	IPR037039	Chorismate mutase, AroQ class superfamily, eukaryotic	Homologous Superfamily

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	chorismate mutase (AroQ) M-CSA #81	Chorismate mutase (CM; EC:5.4.99.5) catalyses the reaction at the branch point of the biosynthetic pathway leading to the three aromatic amino acids, phenylalanine, tryptophan and tyrosine (chorismic acid is the last common intermediate, and CM leads to the L-phenylalanine/L-tyrosine branch). It is part of the shikimate pathway, which is present only in bacteria, fungi and plants. Members of this family, which are restricted to plants and fungi, contain a chorismate mutase domain of the AroQ class (eukaryotic type) and have an all-helical structure. The monomer consists of a catalytic and a regulatory domain covalently linked by a loop, which functions as a molecular hinge. They are monofunctional, allosteric enzymes and are subject to allosteric inhibition by tyrosine and activation by tryptophan.	Defined by 7 residues: ARG:A-16ARG:A-157LYS:A-168ASN:A-194GLU:A-198THR:A-242GLU:A-246 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 5.4.99.5 (PDB Primary Data) Search M-CSA Motif + EC 5.4.99.5

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.