Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6D3Q

Crystal structure of Escherichia coli enolase complexed with a natural inhibitor SF2312.

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
E	0000015	cellular_component	phosphopyruvate hydratase complex
E	0000287	molecular_function	magnesium ion binding
E	0004634	molecular_function	phosphopyruvate hydratase activity
E	0005515	molecular_function	protein binding
E	0005576	cellular_component	extracellular region
E	0005737	cellular_component	cytoplasm
E	0005829	cellular_component	cytosol
E	0005856	cellular_component	cytoskeleton
E	0006096	biological_process	glycolytic process
E	0006396	biological_process	RNA processing
E	0006401	biological_process	RNA catabolic process
E	0009986	cellular_component	cell surface
E	0016020	cellular_component	membrane
E	0016829	molecular_function	lyase activity
E	0042802	molecular_function	identical protein binding
E	0042803	molecular_function	protein homodimerization activity
E	0046872	molecular_function	metal ion binding
E	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	19
Details	binding site for residue 4NG A 501

Chain	Residue
A	GLY39
A	LEU339
A	LYS341
A	HIS369
A	ARG370
A	SER371
A	LYS392
A	MG502
A	MG503
A	HOH638
A	HOH645
A	ALA40
A	SER41
A	GLN166
A	GLU167
A	GLU208
A	ASP245
A	GLU289
A	ASP316

site_id	AC2
Number of Residues	5
Details	binding site for residue MG A 502

Chain	Residue
A	ASP245
A	GLU289
A	ASP316
A	4NG501
A	HOH627

site_id	AC3
Number of Residues	4
Details	binding site for residue MG A 503

Chain	Residue
A	SER41
A	4NG501
A	HOH638
A	HOH645

site_id	AC4
Number of Residues	6
Details	binding site for residue GOL A 504

Chain	Residue
A	ILE94
A	THR99
A	GLU100
A	LYS102
A	LYS324
A	GLU350

site_id	AC5
Number of Residues	18
Details	binding site for residue 4NG C 501

Chain	Residue
C	GLY39
C	ALA40
C	SER41
C	GLN166
C	GLU167
C	GLU208
C	ASP245
C	GLU289
C	ASP316
C	LYS341
C	HIS369
C	ARG370
C	SER371
C	LYS392
C	MG502
C	MG503
C	HOH603
C	HOH616

site_id	AC6
Number of Residues	5
Details	binding site for residue MG C 502

Chain	Residue
C	ASP245
C	GLU289
C	ASP316
C	4NG501
C	HOH609

site_id	AC7
Number of Residues	4
Details	binding site for residue MG C 503

Chain	Residue
C	SER41
C	4NG501
C	HOH603
C	HOH616

site_id	AC8
Number of Residues	6
Details	binding site for residue SO4 C 504

Chain	Residue
A	ARG-3
B	ARG-3
C	ARG-3
C	GLY-4
C	HOH601
F	GLN-6

site_id	AC9
Number of Residues	4
Details	binding site for residue SO4 C 505

Chain	Residue
C	LYS179
C	GLU180
C	ARG183
D	ARG57

site_id	AD1
Number of Residues	19
Details	binding site for residue 4NG B 501

Chain	Residue
B	GLY39
B	ALA40
B	SER41
B	GLN166
B	GLU167
B	GLU208
B	ASP245
B	GLU289
B	ASP316
B	LEU339
B	LYS341
B	HIS369
B	ARG370
B	SER371
B	LYS392
B	MG502
B	MG503
B	HOH645
B	HOH652

site_id	AD2
Number of Residues	5
Details	binding site for residue MG B 502

Chain	Residue
B	ASP245
B	GLU289
B	ASP316
B	4NG501
B	HOH632

site_id	AD3
Number of Residues	4
Details	binding site for residue MG B 503

Chain	Residue
B	SER41
B	4NG501
B	HOH645
B	HOH652

site_id	AD4
Number of Residues	7
Details	binding site for residue GOL B 504

Chain	Residue
B	ILE94
B	THR99
B	GLU100
B	LYS102
B	GLU350
B	HOH612
B	HOH671

site_id	AD5
Number of Residues	3
Details	binding site for residue SO4 B 505

Chain	Residue
A	GLU180
A	ARG183
B	ARG57

site_id	AD6
Number of Residues	4
Details	binding site for residue SO4 B 506

Chain	Residue
A	ARG57
B	GLU180
B	ARG183
B	HOH627

site_id	AD7
Number of Residues	20
Details	binding site for residue 4NG E 501

Chain	Residue
E	GLY39
E	ALA40
E	SER41
E	GLN166
E	GLU167
E	GLU208
E	ASP245
E	GLU289
E	ASP316
E	LEU339
E	LYS341
E	HIS369
E	ARG370
E	SER371
E	LYS392
E	MG502
E	MG503
E	HOH607
E	HOH637
E	HOH641

site_id	AD8
Number of Residues	5
Details	binding site for residue MG E 502

Chain	Residue
E	ASP245
E	GLU289
E	ASP316
E	4NG501
E	HOH637

site_id	AD9
Number of Residues	4
Details	binding site for residue MG E 503

Chain	Residue
E	SER41
E	4NG501
E	HOH607
E	HOH641

site_id	AE1
Number of Residues	7
Details	binding site for residue GOL E 504

Chain	Residue
E	ILE94
E	THR99
E	GLU100
E	LYS102
E	LYS324
E	GLU350
E	HOH609

site_id	AE2
Number of Residues	4
Details	binding site for residue SO4 E 505

Chain	Residue
E	LYS179
E	GLU180
E	ARG183
F	ARG57

site_id	AE3
Number of Residues	4
Details	binding site for residue SO4 E 506

Chain	Residue
E	THR99
E	GLU100
E	ASN101
E	SER103

site_id	AE4
Number of Residues	19
Details	binding site for residue 4NG F 501

Chain	Residue
F	GLY39
F	ALA40
F	SER41
F	GLN166
F	GLU167
F	GLU208
F	ASP245
F	GLU289
F	ASP316
F	LEU339
F	LYS341
F	HIS369
F	ARG370
F	SER371
F	LYS392
F	MG502
F	MG503
F	HOH614
F	HOH640

site_id	AE5
Number of Residues	6
Details	binding site for residue MG F 502

Chain	Residue
F	ASP245
F	GLU289
F	ASP316
F	LYS392
F	4NG501
F	HOH637

site_id	AE6
Number of Residues	4
Details	binding site for residue MG F 503

Chain	Residue
F	SER41
F	4NG501
F	HOH614
F	HOH640

site_id	AE7
Number of Residues	5
Details	binding site for residue GOL F 504

Chain	Residue
F	ILE94
F	THR99
F	GLU100
F	LYS102
F	GLU350

site_id	AE8
Number of Residues	7
Details	binding site for residue SO4 F 505

Chain	Residue
A	ARG-3
A	GLY-4
D	GLN-6
E	ARG-3
F	ARG-3
F	HOH601
F	HOH607

site_id	AE9
Number of Residues	4
Details	binding site for residue SO4 F 506

Chain	Residue
E	ARG57
F	LYS179
F	GLU180
F	ARG183

site_id	AF1
Number of Residues	4
Details	binding site for residue SO4 F 507

Chain	Residue
F	THR99
F	GLU100
F	ASN101
F	SER103

site_id	AF2
Number of Residues	19
Details	binding site for residue 4NG D 501

Chain	Residue
D	GLY39
D	ALA40
D	SER41
D	GLN166
D	GLU167
D	GLU208
D	ASP245
D	GLU289
D	ASP316
D	LEU339
D	LYS341
D	HIS369
D	ARG370
D	SER371
D	LYS392
D	MG502
D	MG503
D	HOH604
D	HOH632

site_id	AF3
Number of Residues	5
Details	binding site for residue MG D 502

Chain	Residue
D	ASP245
D	GLU289
D	ASP316
D	4NG501
D	HOH610

site_id	AF4
Number of Residues	4
Details	binding site for residue MG D 503

Chain	Residue
D	SER41
D	4NG501
D	HOH604
D	HOH632

site_id	AF5
Number of Residues	5
Details	binding site for residue GOL D 504

Chain	Residue
D	ILE94
D	THR99
D	GLU100
D	LYS102
D	GLU350

site_id	AF6
Number of Residues	6
Details	binding site for residue SO4 D 505

Chain	Residue
B	GLN-6
C	ARG-3
D	ARG-3
D	HOH601
E	ARG-3
F	ARG-3

site_id	AF7
Number of Residues	5
Details	binding site for residue SO4 D 506

Chain	Residue
C	ARG57
D	LYS179
D	GLU180
D	ARG183
D	HOH661

site_id	AF8
Number of Residues	3
Details	binding site for residue SO4 D 507

Chain	Residue
D	THR99
D	ASN101
D	SER103

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	6
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_FI2
Number of Residues	6
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_FI3
Number of Residues	30
Details	Binding site: {"evidences":[{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	6
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_FI5
Number of Residues	6
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_FI6
Number of Residues	6
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_FI7
Number of Residues	6
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_FI8
Number of Residues	174
Details	Region: {"description":"Interaction with RNase E"}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	6
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_FI10
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	6
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_FI12
Number of Residues	18
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	6
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	6
Details	Modified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"31328167","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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