Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6BFZ

Crystal structure of enolase from E. coli with a mixture of apo form, substrate, and product form

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
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
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
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
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
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	binding site for residue MG A 601

Chain	Residue
A	ASP245
A	GLU289
A	ASP290
A	ASP316

site_id	AC2
Number of Residues	5
Details	binding site for residue SO4 A 602

Chain	Residue
A	LYS341
A	ARG370
A	SER371
A	HOH701
A	HOH713

site_id	AC3
Number of Residues	4
Details	binding site for residue SO4 A 603

Chain	Residue
A	GLY43
A	SER44
A	ARG45
A	HOH739

site_id	AC4
Number of Residues	3
Details	binding site for residue SO4 A 604

Chain	Residue
A	GLU180
A	ARG183
B	ARG57

site_id	AC5
Number of Residues	4
Details	binding site for residue SO4 A 605

Chain	Residue
A	ARG57
B	LYS179
B	GLU180
B	ARG183

site_id	AC6
Number of Residues	4
Details	binding site for residue MG B 601

Chain	Residue
B	ASP245
B	GLU289
B	ASP290
B	ASP316

site_id	AC7
Number of Residues	2
Details	binding site for residue SO4 B 602

Chain	Residue
B	SER44
B	ARG45

site_id	AC8
Number of Residues	3
Details	binding site for residue SO4 B 603

Chain	Residue
B	LYS341
B	ARG370
B	SER371

site_id	AC9
Number of Residues	8
Details	binding site for residue GOL B 604

Chain	Residue
A	ARG-3
B	ARG-3
B	GLY-4
C	ARG-3
C	GOL505
D	ARG-3
E	GLN-6
F	GLN-6

site_id	AD1
Number of Residues	6
Details	binding site for residue MG E 601

Chain	Residue
E	ASP245
E	GLU289
E	ASP316
E	PEP602
E	2PG603
E	HOH718

site_id	AD2
Number of Residues	5
Details	binding site for residue SO4 E 604

Chain	Residue
E	LYS179
E	GLU180
E	ARG183
E	HOH775
F	ARG57

site_id	AD3
Number of Residues	5
Details	binding site for residue SO4 E 605

Chain	Residue
E	ARG15
E	ASN17
E	LYS61
E	HOH734
F	HIS190

site_id	AD4
Number of Residues	5
Details	binding site for residue MES E 606

Chain	Residue
B	TRP297
B	GLU328
B	LYS332
E	ASP54
E	SER56

site_id	AD5
Number of Residues	16
Details	binding site for residue 2PG 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

site_id	AD6
Number of Residues	5
Details	binding site for residue MG F 502

Chain	Residue
F	ASP245
F	GLU289
F	ASP316
F	2PG501
F	HOH619

site_id	AD7
Number of Residues	4
Details	binding site for residue SO4 F 503

Chain	Residue
E	HIS190
F	ARG15
F	ASN17
F	LYS61

site_id	AD8
Number of Residues	4
Details	binding site for residue SO4 F 504

Chain	Residue
E	ARG57
F	GLU180
F	ARG183
F	HOH675

site_id	AD9
Number of Residues	6
Details	binding site for residue GOL F 505

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

site_id	AE1
Number of Residues	16
Details	binding site for residue 2PG D 501

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

site_id	AE2
Number of Residues	5
Details	binding site for residue MG D 502

Chain	Residue
D	ASP245
D	GLU289
D	ASP316
D	2PG501
D	HOH611

site_id	AE3
Number of Residues	4
Details	binding site for residue SO4 D 503

Chain	Residue
C	HIS190
D	ARG15
D	ASN17
D	LYS61

site_id	AE4
Number of Residues	5
Details	binding site for residue MES D 504

Chain	Residue
A	TRP297
A	GLU328
A	LYS332
D	ASP54
D	LYS55

site_id	AE5
Number of Residues	16
Details	binding site for residue 2PG C 501

Chain	Residue
C	GLY39
C	ALA40
C	SER41
C	GLN166
C	GLU167
C	GLU208
C	ASP245
C	GLU289
C	ASP316
C	LEU339
C	LYS341
C	HIS369
C	ARG370
C	SER371
C	LYS392
C	MG502

site_id	AE6
Number of Residues	5
Details	binding site for residue MG C 502

Chain	Residue
C	ASP245
C	GLU289
C	ASP316
C	2PG501
C	HOH636

site_id	AE7
Number of Residues	3
Details	binding site for residue SO4 C 503

Chain	Residue
C	ARG57
D	GLU180
D	ARG183

site_id	AE8
Number of Residues	3
Details	binding site for residue SO4 C 504

Chain	Residue
C	GLU180
C	ARG183
D	ARG57

site_id	AE9
Number of Residues	7
Details	binding site for residue GOL C 505

Chain	Residue
B	GLN-6
B	GOL604
C	ARG-3
D	ARG-3
E	ARG-3
E	GLY-4
F	ARG-3

site_id	AF1
Number of Residues	17
Details	binding site for residues PEP E 602 and 2PG E 603

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	MG601
E	HOH701

site_id	AF2
Number of Residues	17
Details	binding site for residues PEP E 602 and 2PG E 603

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	MG601
E	HOH701

site_id	AF3
Number of Residues	17
Details	binding site for residues PEP E 602 and 2PG E 603

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	MG601
E	HOH701

site_id	AF4
Number of Residues	17
Details	binding site for residues PEP E 602 and 2PG E 603

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	MG601
E	HOH701

site_id	AF5
Number of Residues	17
Details	binding site for residues PEP E 602 and 2PG E 603

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	MG601
E	HOH701

site_id	AF6
Number of Residues	17
Details	binding site for residues PEP E 602 and 2PG E 603

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	MG601
E	HOH701

site_id	AF7
Number of Residues	17
Details	binding site for residues PEP E 602 and 2PG E 603

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	MG601
E	HOH701

site_id	AF8
Number of Residues	17
Details	binding site for residues PEP E 602 and 2PG E 603

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	MG601
E	HOH701

site_id	AF9
Number of Residues	17
Details	binding site for residues PEP E 602 and 2PG E 603

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	MG601
E	HOH701

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	11
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)