Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1E9I

Enolase from E.coli

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
B	0000015	cellular_component	phosphopyruvate hydratase complex
B	0000287	molecular_function	magnesium ion binding
B	0004634	molecular_function	phosphopyruvate hydratase activity
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005856	cellular_component	cytoskeleton
B	0006096	biological_process	glycolytic process
B	0006396	biological_process	RNA processing
B	0006401	biological_process	RNA catabolic process
B	0009986	cellular_component	cell surface
B	0016020	cellular_component	membrane
B	0016829	molecular_function	lyase activity
B	0042802	molecular_function	identical protein binding
B	0042803	molecular_function	protein homodimerization activity
B	0046872	molecular_function	metal ion binding
B	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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A1431

Chain	Residue
A	ASP245
A	GLU289
A	ASP316
A	HOH2052
A	HOH2080
A	HOH2095

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B1431

Chain	Residue
B	HOH2086
B	HOH2087
B	ASP245
B	GLU289
B	ASP316

site_id	AC3
Number of Residues	8
Details	BINDING SITE FOR RESIDUE MG C1429

Chain	Residue
C	ASP245
C	GLU289
C	ASP316
C	LYS392
C	HOH2077
C	HOH2080
C	HOH2082
C	HOH2098

site_id	AC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG D1432

Chain	Residue
D	ASP245
D	GLU289
D	ASP290
D	ASP316
D	MG1433
D	HOH2082
D	HOH2114

site_id	AC5
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG D1433

Chain	Residue
D	SER41
D	ASP316
D	MG1432
D	SO41434
D	HOH2108
D	HOH2109

site_id	AC6
Number of Residues	10
Details	BINDING SITE FOR RESIDUE SO4 D1434

Chain	Residue
D	GLY39
D	ALA40
D	SER41
D	HIS158
D	GLN166
D	LYS341
D	ARG370
D	SER371
D	MG1433
D	HOH2109

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	4
Details	ACT_SITE: Proton donor => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0000269\|PubMed:15003462

Chain	Residue	Details
A	GLY209
B	GLY209
C	GLY209
D	GLY209

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0000269\|PubMed:15003462

Chain	Residue	Details
A	PHE342
B	PHE342
C	PHE342
D	PHE342

site_id	SWS_FT_FI3
Number of Residues	20
Details	BINDING: BINDING => ECO:0007744\|PDB:6BFZ

Chain	Residue	Details
A	GLU167
C	PHE342
C	SER371
C	GLY372
D	GLU167
D	PHE342
D	SER371
D	GLY372
A	SER41
B	SER41
C	SER41
A	PHE342
D	SER41
A	SER371
A	GLY372
B	GLU167
B	PHE342
B	SER371
B	GLY372
C	GLU167

site_id	SWS_FT_FI4
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0000269\|PubMed:11676541, ECO:0000269\|PubMed:16516921, ECO:0000269\|PubMed:20823555, ECO:0007744\|PDB:1E9I, ECO:0007744\|PDB:2FYM, ECO:0007744\|PDB:3H8A, ECO:0007744\|PDB:6BFY, ECO:0007744\|PDB:6BFZ

Chain	Residue	Details
A	CYS246
B	CYS246
C	CYS246
D	CYS246

site_id	SWS_FT_FI5
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0000269\|PubMed:11676541, ECO:0000269\|PubMed:20823555, ECO:0000269\|PubMed:30714720, ECO:0007744\|PDB:1E9I, ECO:0007744\|PDB:2FYM, ECO:0007744\|PDB:3H8A, ECO:0007744\|PDB:6BFY, ECO:0007744\|PDB:6BFZ

Chain	Residue	Details
A	ASP290
B	ASP290
C	ASP290
D	ASP290

site_id	SWS_FT_FI6
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0000269\|PubMed:11676541, ECO:0000269\|PubMed:16516921, ECO:0000269\|PubMed:20823555, ECO:0007744\|PDB:1E9I, ECO:0007744\|PDB:2FYM, ECO:0007744\|PDB:6BFY, ECO:0007744\|PDB:6BFZ

Chain	Residue	Details
A	ASP317
B	ASP317
C	ASP317
D	ASP317

site_id	SWS_FT_FI7
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0007744\|PDB:6BFY, ECO:0007744\|PDB:6BFZ

Chain	Residue	Details
A	THR393
B	THR393
C	THR393
D	THR393

site_id	SWS_FT_FI8
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269\|PubMed:30714720, ECO:0007744\|PDB:6BFY

Chain	Residue	Details
A	THR42
B	THR42
C	THR42
D	THR42

site_id	SWS_FT_FI9
Number of Residues	8
Details	BINDING: BINDING => ECO:0007744\|PDB:6BFY

Chain	Residue	Details
A	ALA159
A	GLY209
B	ALA159
B	GLY209
C	ALA159
C	GLY209
D	ALA159
D	GLY209

site_id	SWS_FT_FI10
Number of Residues	4
Details	BINDING: BINDING => ECO:0007744\|PDB:6BFY, ECO:0007744\|PDB:6BFZ

Chain	Residue	Details
A	PHE168
B	PHE168
C	PHE168
D	PHE168

site_id	SWS_FT_FI11
Number of Residues	12
Details	SITE: Interaction with RNase E => ECO:0000269\|PubMed:16516921, ECO:0000269\|PubMed:20823555

Chain	Residue	Details
A	ALA120
D	ALA120
D	ASP376
D	LEU408
A	ASP376
A	LEU408
B	ALA120
B	ASP376
B	LEU408
C	ALA120
C	ASP376
C	LEU408

site_id	SWS_FT_FI12
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842

Chain	Residue	Details
A	TYR257
B	TYR257
C	TYR257
D	TYR257

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:31328167

Chain	Residue	Details
A	PHE342
B	PHE342
C	PHE342
D	PHE342

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
B	HIS191
B	LYS341

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

Chain	Residue	Details
C	HIS191
C	LYS341

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

Chain	Residue	Details
D	HIS191
D	LYS341

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

Chain	Residue	Details
B	LYS392
B	GLU208
B	HIS369
B	GLU167

site_id	CSA3
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	CSA4
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	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
B	GLU208
B	GLU167
B	HIS369
B	LYS341

site_id	CSA7
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	CSA8
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	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)