7ENL

MECHANISM OF ENOLASE: THE CRYSTAL STRUCTURE OF ENOLASE-MG2+-PHOSPHOGLYCERATE(SLASH) PHOSPHOENOLPYRUVATE COMPLEX AT 2.2-ANGSTROMS 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
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	d7enla1	Alpha and beta proteins (a/b)	TIM beta/alpha-barrel	Enolase C-terminal domain-like	Enolase	Enolase	baker's yeast (Saccharomyces cerevisiae ) [TaxId: 4932 ],	SCOPe (2.08)
A	d7enla2	Alpha and beta proteins (a+b)	Enolase N-terminal domain-like	Enolase N-terminal domain-like	Enolase N-terminal domain-like	Enolase	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	Enolase C-terminal domain-like	8037169	3000476	SCOP2B (2022-06-29)
A	SCOP2B Superfamily	Enolase N-terminal domain-like	8037167	3001064	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	PF03952	e7enlA1	A: a+b two layers	X: Enolase-N/ribosomal protein	H: Enolase N-terminal domain-like (From Topology)	T: Enolase N-terminal domain-like	F: PF03952	ECOD (1.6)
A	PF00113	e7enlA2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: PF00113	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.390.10	Alpha Beta	2-Layer Sandwich	Enolase-like	domain 1	CATH (4.3.0)
A	3.20.20.120	Alpha Beta	Alpha-Beta Barrel	TIM Barrel	Enolase-like C-terminal domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF00113	Enolase, C-terminal TIM barrel domain (Enolase_C)	Enolase, C-terminal TIM barrel domain	-	Domain
A	PF03952	Enolase, N-terminal domain (Enolase_N)	Enolase, N-terminal domain	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	ENOLASE	cation binding magnesium ion binding ion binding binding metal ion binding small molecule binding hydro-lyase activity lyase activity phosphopyruvate hydratase activity catalytic activity carbon-oxygen lyase activity melatonin binding amide binding organic cyclic compound binding	ribonucleotide catabolic process pyridine nucleotide catabolic process oxoacid metabolic process carbohydrate catabolic process carbohydrate derivative metabolic process organophosphate catabolic process nucleoside phosphate catabolic process organic acid metabolic process nucleobase-containing compound metabolic process glycolytic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process purine ribonucleotide catabolic process ribonucleotide catabolic process pyridine nucleotide catabolic process oxoacid metabolic process carbohydrate catabolic process carbohydrate derivative metabolic process organophosphate catabolic process nucleoside phosphate catabolic process organic acid metabolic process nucleobase-containing compound metabolic process glycolytic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process small molecule metabolic process purine ribonucleotide catabolic process phosphorus metabolic process pyridine nucleotide metabolic process nucleoside phosphate metabolic process organonitrogen compound catabolic process nicotinamide nucleotide metabolic process pyruvate metabolic process cellular metabolic process purine nucleoside diphosphate metabolic process primary metabolic process purine-containing compound catabolic process nucleotide metabolic process nucleobase-containing compound catabolic process organic cyclic compound metabolic process nucleoside diphosphate metabolic process purine nucleoside diphosphate catabolic process nucleoside diphosphate catabolic process metabolic process nucleoside triphosphate metabolic process monocarboxylic acid metabolic process purine ribonucleotide metabolic process pyridine-containing compound catabolic process ribose phosphate metabolic process catabolic process ATP metabolic process purine nucleotide metabolic process organic substance metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process purine ribonucleoside triphosphate metabolic process ribonucleoside diphosphate metabolic process ribonucleoside diphosphate catabolic process nucleotide catabolic process ribonucleoside triphosphate metabolic process purine nucleoside triphosphate metabolic process purine nucleotide catabolic process carbohydrate metabolic process carbohydrate derivative catabolic process organonitrogen compound metabolic process ADP catabolic process carboxylic acid metabolic process generation of precursor metabolites and energy organic cyclic compound catabolic process purine-containing compound metabolic process ADP metabolic process organophosphate metabolic process purine ribonucleoside diphosphate metabolic process cellular process organic substance catabolic process purine ribonucleoside diphosphate catabolic process regulation of biological process regulation of cellular component organization regulation of cellular process vacuole organization biological regulation regulation of vacuole organization regulation of organelle organization cellular component organization organelle fusion organelle organization vacuole fusion vacuole fusion, non-autophagic regulation of vacuole fusion, non-autophagic cellular component organization or biogenesis	membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle storage vacuole lytic vacuole vacuole fungal-type vacuole cytosol cell periphery membrane-bounded organelle intracellular organelle intracellular anatomical structure mitochondrion organelle cytoplasm cellular anatomical entity intracellular membrane-bounded organelle storage vacuole lytic vacuole vacuole fungal-type vacuole cytosol cell periphery plasma membrane membrane protein-containing complex catalytic complex phosphopyruvate hydratase complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036849	Enolase-like, C-terminal domain superfamily	Homologous Superfamily
A	IPR020809	Enolase, conserved site	Conserved Site
A	IPR020810	Enolase, C-terminal TIM barrel domain	Domain
A	IPR020811	Enolase, N-terminal	Domain
A	IPR000941	Enolase	Family
A	IPR029017	Enolase-like, N-terminal	Homologous Superfamily

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

Chains	Enzyme Name	Description	Catalytic Residues
A	phosphopyruvate hydratase M-CSA #311	Yeast enolase (2-phospho-D-glycerate hydrolase) is a metalloenzyme which catalyses the reversible dehydration of D-2-phos-phoglycerate (PGA) to phosphoenolpyruvate (PEP). The enzyme has an absolute requirement for the presence of a divalent cation, as is characteristic of the enolase family. Mitochondrial targeting of tRK1 in yeast is achieved by the successive actions of enolase 2 and the precursor of the mitochondrial lysyl-tRNA synthetase (preMSK). At the mitochondrial outer membrane, preMSK takes over enolase to start the import process properly; A fraction of the canonical tRNA L-form tRK1 pool is deviated from the cytosolic translation process by the enolase 2, which favours the tRNA conformational change leading to the formation of the F-form.	Defined by 10 residues: SER:A-39HIS:A-159GLU:A-168GLU:A-211ASP:A-246GLU:A-295ASP:A-320LYS:A-345HIS:A-373LYS:A-396 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 4.2.1.11 (PDB Primary Data) Search M-CSA Motif + EC 4.2.1.11

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.