Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2FYM

Crystal structure of E. coli enolase complexed with the minimal binding segment of RNase E.

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000015	cellular_component	phosphopyruvate hydratase complex
A	0000287	molecular_function	magnesium ion binding
A	0004634	molecular_function	phosphopyruvate hydratase activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005856	cellular_component	cytoskeleton
A	0006096	biological_process	glycolytic process
A	0006396	biological_process	RNA processing
A	0006401	biological_process	RNA catabolic process
A	0009986	cellular_component	cell surface
A	0016020	cellular_component	membrane
A	0016829	molecular_function	lyase activity
A	0042802	molecular_function	identical protein binding
A	0042803	molecular_function	protein homodimerization activity
A	0046872	molecular_function	metal ion binding
A	1990061	cellular_component	bacterial degradosome
C	0000015	cellular_component	phosphopyruvate hydratase complex
C	0000287	molecular_function	magnesium ion binding
C	0004634	molecular_function	phosphopyruvate hydratase activity
C	0005515	molecular_function	protein binding
C	0005576	cellular_component	extracellular region
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005856	cellular_component	cytoskeleton
C	0006096	biological_process	glycolytic process
C	0006396	biological_process	RNA processing
C	0006401	biological_process	RNA catabolic process
C	0009986	cellular_component	cell surface
C	0016020	cellular_component	membrane
C	0016829	molecular_function	lyase activity
C	0042802	molecular_function	identical protein binding
C	0042803	molecular_function	protein homodimerization activity
C	0046872	molecular_function	metal ion binding
C	1990061	cellular_component	bacterial degradosome
D	0000015	cellular_component	phosphopyruvate hydratase complex
D	0000287	molecular_function	magnesium ion binding
D	0004634	molecular_function	phosphopyruvate hydratase activity
D	0005515	molecular_function	protein binding
D	0005576	cellular_component	extracellular region
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005856	cellular_component	cytoskeleton
D	0006096	biological_process	glycolytic process
D	0006396	biological_process	RNA processing
D	0006401	biological_process	RNA catabolic process
D	0009986	cellular_component	cell surface
D	0016020	cellular_component	membrane
D	0016829	molecular_function	lyase activity
D	0042802	molecular_function	identical protein binding
D	0042803	molecular_function	protein homodimerization activity
D	0046872	molecular_function	metal ion binding
D	1990061	cellular_component	bacterial degradosome
F	0000015	cellular_component	phosphopyruvate hydratase complex
F	0000287	molecular_function	magnesium ion binding
F	0004634	molecular_function	phosphopyruvate hydratase activity
F	0005515	molecular_function	protein binding
F	0005576	cellular_component	extracellular region
F	0005737	cellular_component	cytoplasm
F	0005829	cellular_component	cytosol
F	0005856	cellular_component	cytoskeleton
F	0006096	biological_process	glycolytic process
F	0006396	biological_process	RNA processing
F	0006401	biological_process	RNA catabolic process
F	0009986	cellular_component	cell surface
F	0016020	cellular_component	membrane
F	0016829	molecular_function	lyase activity
F	0042802	molecular_function	identical protein binding
F	0042803	molecular_function	protein homodimerization activity
F	0046872	molecular_function	metal ion binding
F	1990061	cellular_component	bacterial degradosome

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 1431

Chain	Residue
A	ASP245
A	GLU289
A	ASP316
A	HOH1442
A	HOH1729
A	HOH1863

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1431

Chain	Residue
C	HOH1445
C	HOH1835
C	ASP245
C	GLU289
C	ASP316

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 1431

Chain	Residue
D	ASP245
D	GLU289
D	ASP316
D	HOH1475
D	HOH1868

site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG F 1431

Chain	Residue
F	ASP245
F	GLU289
F	ASP316
F	HOH1478
F	HOH1569
F	HOH1573

Functional Information from PROSITE/UniProt

site_id	PS00164
Number of Residues	14
Details	ENOLASE Enolase signature. ILIKfNQIGSLTET

Chain	Residue	Details
A	ILE338-THR351

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	116
Details	Region: {"description":"Interaction with RNase E"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15003462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15003462","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	20
Details	Binding site: {"evidences":[{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"30714720","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11676541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16516921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H8A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11676541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30714720","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H8A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11676541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16516921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	12
Details	Site: {"description":"Interaction with RNase E","evidences":[{"source":"PubMed","id":"16516921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"31328167","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	LYS392
A	GLU208
A	HIS369
A	GLU167

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	HIS191
C	LYS341

site_id	CSA11
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	HIS191
D	LYS341

site_id	CSA12
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
F	HIS191
F	LYS341

site_id	CSA2
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	LYS392
C	GLU208
C	HIS369
C	GLU167

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	LYS392
D	GLU208
D	HIS369
D	GLU167

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
F	LYS392
F	GLU208
F	HIS369
F	GLU167

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	GLU208
A	GLU167
A	HIS369
A	LYS341

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	GLU208
C	GLU167
C	HIS369
C	LYS341

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	GLU208
D	GLU167
D	HIS369
D	LYS341

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
F	GLU208
F	GLU167
F	HIS369
F	LYS341

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	HIS191
A	LYS341

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)