Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6NPF

Structure of E.coli enolase in complex with an analog of the natural product SF-2312 metabolite.

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	17
Details	binding site for residue TLA A 601

Chain	Residue
A	GLY39
A	LYS341
A	ARG370
A	SER371
A	LYS392
A	MG603
A	HOH701
A	HOH706
A	HOH712
A	ALA40
A	SER41
A	GLN166
A	GLU167
A	ASP245
A	GLU289
A	ASP316
A	LEU339

site_id	AC2
Number of Residues	4
Details	binding site for residue SO4 A 602

Chain	Residue
A	LYS179
A	GLU180
A	ARG183
B	ARG57

site_id	AC3
Number of Residues	5
Details	binding site for residue MG A 603

Chain	Residue
A	ASP245
A	GLU289
A	ASP316
A	TLA601
A	HOH712

site_id	AC4
Number of Residues	4
Details	binding site for residue SO4 A 604

Chain	Residue
A	ARG57
B	LYS179
B	GLU180
B	ARG183

site_id	AC5
Number of Residues	2
Details	binding site for residue GOL A 605

Chain	Residue
A	HOH702
B	GOL503

site_id	AC6
Number of Residues	16
Details	binding site for residue TLA 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	ARG370
B	SER371
B	LYS392
B	MG502
B	HOH605

site_id	AC7
Number of Residues	5
Details	binding site for residue MG B 502

Chain	Residue
B	ASP245
B	GLU289
B	ASP316
B	TLA501
B	HOH605

site_id	AC8
Number of Residues	1
Details	binding site for residue GOL B 503

Chain	Residue
A	GOL605

site_id	AC9
Number of Residues	5
Details	binding site for residue SO4 B 504

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

site_id	AD1
Number of Residues	4
Details	binding site for residue SO4 C 701

Chain	Residue
C	LYS179
C	GLU180
C	ARG183
D	ARG57

site_id	AD2
Number of Residues	6
Details	binding site for residue MG C 702

Chain	Residue
C	ASP245
C	GLU289
C	ASP290
C	ASP316
C	TLA703
C	HOH807

site_id	AD3
Number of Residues	17
Details	binding site for residue TLA C 703

Chain	Residue
C	GLY39
C	ALA40
C	SER41
C	HIS158
C	GLN166
C	GLU167
C	ASP245
C	GLU289
C	ASP316
C	LYS341
C	ARG370
C	SER371
C	LYS392
C	MG702
C	HOH804
C	HOH807
C	HOH815

site_id	AD4
Number of Residues	2
Details	binding site for residue SO4 C 704

Chain	Residue
C	LYS428
C	GLY429

site_id	AD5
Number of Residues	3
Details	binding site for residue GOL C 705

Chain	Residue
A	HOH743
C	MET-5
C	HOH823

site_id	AD6
Number of Residues	16
Details	binding site for residue KVM D 601

Chain	Residue
D	ASP316
D	LEU339
D	LYS341
D	HIS369
D	ARG370
D	SER371
D	LYS392
D	MG604
D	GLY39
D	ALA40
D	SER41
D	GLN166
D	GLU167
D	GLU208
D	ASP245
D	GLU289

site_id	AD7
Number of Residues	3
Details	binding site for residue SO4 D 602

Chain	Residue
C	ARG57
D	GLU180
D	ARG183

site_id	AD8
Number of Residues	6
Details	binding site for residue SO4 D 603

Chain	Residue
A	GLN-6
D	ARG-3
D	GLY-4
D	HOH702
E	ARG-3
F	ARG-3

site_id	AD9
Number of Residues	5
Details	binding site for residue MG D 604

Chain	Residue
D	ASP245
D	GLU289
D	ASP316
D	KVM601
D	HOH711

site_id	AE1
Number of Residues	6
Details	binding site for residue GOL D 605

Chain	Residue
D	HOH705
D	HOH713
D	HOH724
D	HOH727
D	HOH731
D	HOH742

site_id	AE2
Number of Residues	5
Details	binding site for residue SO4 D 606

Chain	Residue
D	GLU21
D	MET33
D	ALA35
D	GLU375
D	ASP376

site_id	AE3
Number of Residues	4
Details	binding site for residue SO4 F 701

Chain	Residue
E	ARG57
F	LYS179
F	GLU180
F	ARG183

site_id	AE4
Number of Residues	5
Details	binding site for residue MG F 702

Chain	Residue
F	ASP245
F	GLU289
F	ASP316
F	KVM703
F	HOH811

site_id	AE5
Number of Residues	17
Details	binding site for residue KVM F 703

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	MG702
F	HOH811

site_id	AE6
Number of Residues	2
Details	binding site for residue SO4 F 704

Chain	Residue
E	ARG183
F	ARG57

site_id	AE7
Number of Residues	5
Details	binding site for residue SO4 F 705

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

site_id	AE8
Number of Residues	6
Details	binding site for residue MG E 601

Chain	Residue
E	ASP245
E	GLU289
E	ASP316
E	LYS392
E	KVM602
E	HOH701

site_id	AE9
Number of Residues	15
Details	binding site for residue KVM E 602

Chain	Residue
E	GLY39
E	ALA40
E	SER41
E	GLN166
E	GLU167
E	GLU208
E	ASP245
E	ASP316
E	LYS341
E	ARG370
E	SER371
E	LYS392
E	MG601
E	HOH701
E	HOH708

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

Chain	Residue	Details
A	GLU208
B	GLU208
C	GLU208
D	GLU208
F	GLU208
E	GLU208

site_id	SWS_FT_FI2
Number of Residues	6
Details	ACT_SITE: Proton acceptor => ECO:0000255\|HAMAP-Rule:MF_00318, ECO:0000269\|PubMed:15003462

Chain	Residue	Details
A	LYS341
B	LYS341
C	LYS341
D	LYS341
F	LYS341
E	LYS341

site_id	SWS_FT_FI3
Number of Residues	30
Details	BINDING: BINDING => ECO:0007744\|PDB:6BFZ

Chain	Residue	Details
A	GLN166
C	LYS341
C	ARG370
C	SER371
D	GLN166
D	LYS341
D	ARG370
D	SER371
F	GLN166
F	LYS341
F	ARG370
A	LYS341
F	SER371
E	GLN166
E	LYS341
E	ARG370
E	SER371
A	ALA40
B	ALA40
C	ALA40
D	ALA40
F	ALA40
A	ARG370
E	ALA40
A	SER371
B	GLN166
B	LYS341
B	ARG370
B	SER371
C	GLN166

site_id	SWS_FT_FI4
Number of Residues	6
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	ASP245
B	ASP245
C	ASP245
D	ASP245
F	ASP245
E	ASP245

site_id	SWS_FT_FI5
Number of Residues	6
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	GLU289
B	GLU289
C	GLU289
D	GLU289
F	GLU289
E	GLU289

site_id	SWS_FT_FI6
Number of Residues	6
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	ASP316
B	ASP316
C	ASP316
D	ASP316
F	ASP316
E	ASP316

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

Chain	Residue	Details
A	LYS392
B	LYS392
C	LYS392
D	LYS392
F	LYS392
E	LYS392

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

Chain	Residue	Details
A	SER41
B	SER41
C	SER41
D	SER41
F	SER41
E	SER41

site_id	SWS_FT_FI9
Number of Residues	12
Details	BINDING: BINDING => ECO:0007744\|PDB:6BFY

Chain	Residue	Details
A	HIS158
F	GLU208
E	HIS158
E	GLU208
A	GLU208
B	HIS158
B	GLU208
C	HIS158
C	GLU208
D	HIS158
D	GLU208
F	HIS158

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

Chain	Residue	Details
A	GLU167
B	GLU167
C	GLU167
D	GLU167
F	GLU167
E	GLU167

site_id	SWS_FT_FI11
Number of Residues	18
Details	SITE: Interaction with RNase E => ECO:0000269\|PubMed:16516921, ECO:0000269\|PubMed:20823555

Chain	Residue	Details
A	LYS119
D	LYS119
D	GLU375
D	GLN407
F	LYS119
F	GLU375
F	GLN407
E	LYS119
E	GLU375
E	GLN407
A	GLU375
A	GLN407
B	LYS119
B	GLU375
B	GLN407
C	LYS119
C	GLU375
C	GLN407

site_id	SWS_FT_FI12
Number of Residues	6
Details	MOD_RES: N6-acetyllysine => ECO:0000269\|PubMed:18723842

Chain	Residue	Details
A	LYS256
B	LYS256
C	LYS256
D	LYS256
F	LYS256
E	LYS256

site_id	SWS_FT_FI13
Number of Residues	6
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269\|PubMed:31328167

Chain	Residue	Details
A	LYS341
B	LYS341
C	LYS341
D	LYS341
F	LYS341
E	LYS341

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