Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

5OHG

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

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue MG A 501

Chain	Residue
A	ASP246
A	GLU290
A	ASP317
A	LYS342
A	HOH611
A	HOH632

site_id	AC2
Number of Residues	6
Details	binding site for residue NA A 502

Chain	Residue
A	ASN162
A	VAL164
A	HOH918
A	GLY156
A	GLY157
A	ALA160

site_id	AC3
Number of Residues	8
Details	binding site for residue PO4 A 503

Chain	Residue
A	GLY40
A	ALA41
A	SER42
A	HIS159
A	GLN167
A	LYS342
A	ARG371
A	SER372

site_id	AC4
Number of Residues	5
Details	binding site for residue MG B 501

Chain	Residue
B	ASP246
B	GLU290
B	ASP317
B	HOH616
B	HOH619

site_id	AC5
Number of Residues	6
Details	binding site for residue NA B 502

Chain	Residue
B	GLY156
B	GLY157
B	ALA160
B	ASN162
B	VAL164
B	HOH873

site_id	AC6
Number of Residues	8
Details	binding site for residue PO4 B 503

Chain	Residue
B	GLY40
B	ALA41
B	SER42
B	HIS159
B	GLN167
B	LYS342
B	ARG371
B	SER372

site_id	AC7
Number of Residues	6
Details	binding site for residue MG H 501

Chain	Residue
H	ASP246
H	GLU290
H	ASP317
H	LYS342
H	HOH603
H	HOH673

site_id	AC8
Number of Residues	5
Details	binding site for residue NA H 502

Chain	Residue
H	GLY157
H	ALA160
H	ASN162
H	VAL164
H	HOH927

site_id	AC9
Number of Residues	8
Details	binding site for residue PO4 H 503

Chain	Residue
H	GLY40
H	ALA41
H	SER42
H	HIS159
H	GLN167
H	LYS342
H	ARG371
H	SER372

site_id	AD1
Number of Residues	6
Details	binding site for residue MG I 501

Chain	Residue
I	ASP246
I	GLU290
I	ASP317
I	LYS342
I	HOH616
I	HOH621

site_id	AD2
Number of Residues	7
Details	binding site for residue NA I 502

Chain	Residue
I	ASP53
I	ASP55
I	ARG58
I	GLY61
I	LYS62
I	GLY63
I	HOH701

site_id	AD3
Number of Residues	5
Details	binding site for residue NA I 503

Chain	Residue
I	GLY157
I	ALA160
I	ASN162
I	VAL164
I	HOH873

site_id	AD4
Number of Residues	8
Details	binding site for residue PO4 I 504

Chain	Residue
I	GLY40
I	ALA41
I	SER42
I	HIS159
I	GLN167
I	LYS342
I	ARG371
I	SER372

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ILE339-THR352

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

site_id	SWS_FT_FI15
Number of Residues	17
Details	Region: {"description":"Interaction with enolase"}

Chain

Residue

Details

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