Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2PSN

Crystal structure of enolase1

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000015	cellular_component	phosphopyruvate hydratase complex
A	0000122	biological_process	negative regulation of transcription by RNA polymerase II
A	0000287	molecular_function	magnesium ion binding
A	0000977	molecular_function	RNA polymerase II transcription regulatory region sequence-specific DNA binding
A	0001222	molecular_function	transcription corepressor binding
A	0001227	molecular_function	DNA-binding transcription repressor activity, RNA polymerase II-specific
A	0003677	molecular_function	DNA binding
A	0003714	molecular_function	transcription corepressor activity
A	0003723	molecular_function	RNA binding
A	0004634	molecular_function	phosphopyruvate hydratase activity
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005640	cellular_component	nuclear outer membrane
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005938	cellular_component	cell cortex
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0009615	biological_process	response to virus
A	0009986	cellular_component	cell surface
A	0010756	biological_process	positive regulation of plasminogen activation
A	0016020	cellular_component	membrane
A	0016829	molecular_function	lyase activity
A	0030308	biological_process	negative regulation of cell growth
A	0031430	cellular_component	M band
A	0042803	molecular_function	protein homodimerization activity
A	0045296	molecular_function	cadherin binding
A	0045892	biological_process	negative regulation of DNA-templated transcription
A	0045933	biological_process	positive regulation of muscle contraction
A	0046872	molecular_function	metal ion binding
A	0051020	molecular_function	GTPase binding
A	0061621	biological_process	canonical glycolysis
A	0070062	cellular_component	extracellular exosome
A	1903298	biological_process	negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
A	2001171	biological_process	positive regulation of ATP biosynthetic process
B	0000015	cellular_component	phosphopyruvate hydratase complex
B	0000122	biological_process	negative regulation of transcription by RNA polymerase II
B	0000287	molecular_function	magnesium ion binding
B	0000977	molecular_function	RNA polymerase II transcription regulatory region sequence-specific DNA binding
B	0001222	molecular_function	transcription corepressor binding
B	0001227	molecular_function	DNA-binding transcription repressor activity, RNA polymerase II-specific
B	0003677	molecular_function	DNA binding
B	0003714	molecular_function	transcription corepressor activity
B	0003723	molecular_function	RNA binding
B	0004634	molecular_function	phosphopyruvate hydratase activity
B	0005515	molecular_function	protein binding
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005640	cellular_component	nuclear outer membrane
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0005938	cellular_component	cell cortex
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0009615	biological_process	response to virus
B	0009986	cellular_component	cell surface
B	0010756	biological_process	positive regulation of plasminogen activation
B	0016020	cellular_component	membrane
B	0016829	molecular_function	lyase activity
B	0030308	biological_process	negative regulation of cell growth
B	0031430	cellular_component	M band
B	0042803	molecular_function	protein homodimerization activity
B	0045296	molecular_function	cadherin binding
B	0045892	biological_process	negative regulation of DNA-templated transcription
B	0045933	biological_process	positive regulation of muscle contraction
B	0046872	molecular_function	metal ion binding
B	0051020	molecular_function	GTPase binding
B	0061621	biological_process	canonical glycolysis
B	0070062	cellular_component	extracellular exosome
B	1903298	biological_process	negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
B	2001171	biological_process	positive regulation of ATP biosynthetic process
C	0000015	cellular_component	phosphopyruvate hydratase complex
C	0000122	biological_process	negative regulation of transcription by RNA polymerase II
C	0000287	molecular_function	magnesium ion binding
C	0000977	molecular_function	RNA polymerase II transcription regulatory region sequence-specific DNA binding
C	0001222	molecular_function	transcription corepressor binding
C	0001227	molecular_function	DNA-binding transcription repressor activity, RNA polymerase II-specific
C	0003677	molecular_function	DNA binding
C	0003714	molecular_function	transcription corepressor activity
C	0003723	molecular_function	RNA binding
C	0004634	molecular_function	phosphopyruvate hydratase activity
C	0005515	molecular_function	protein binding
C	0005615	cellular_component	extracellular space
C	0005634	cellular_component	nucleus
C	0005640	cellular_component	nuclear outer membrane
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0005886	cellular_component	plasma membrane
C	0005938	cellular_component	cell cortex
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0009615	biological_process	response to virus
C	0009986	cellular_component	cell surface
C	0010756	biological_process	positive regulation of plasminogen activation
C	0016020	cellular_component	membrane
C	0016829	molecular_function	lyase activity
C	0030308	biological_process	negative regulation of cell growth
C	0031430	cellular_component	M band
C	0042803	molecular_function	protein homodimerization activity
C	0045296	molecular_function	cadherin binding
C	0045892	biological_process	negative regulation of DNA-templated transcription
C	0045933	biological_process	positive regulation of muscle contraction
C	0046872	molecular_function	metal ion binding
C	0051020	molecular_function	GTPase binding
C	0061621	biological_process	canonical glycolysis
C	0070062	cellular_component	extracellular exosome
C	1903298	biological_process	negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
C	2001171	biological_process	positive regulation of ATP biosynthetic process
D	0000015	cellular_component	phosphopyruvate hydratase complex
D	0000122	biological_process	negative regulation of transcription by RNA polymerase II
D	0000287	molecular_function	magnesium ion binding
D	0000977	molecular_function	RNA polymerase II transcription regulatory region sequence-specific DNA binding
D	0001222	molecular_function	transcription corepressor binding
D	0001227	molecular_function	DNA-binding transcription repressor activity, RNA polymerase II-specific
D	0003677	molecular_function	DNA binding
D	0003714	molecular_function	transcription corepressor activity
D	0003723	molecular_function	RNA binding
D	0004634	molecular_function	phosphopyruvate hydratase activity
D	0005515	molecular_function	protein binding
D	0005615	cellular_component	extracellular space
D	0005634	cellular_component	nucleus
D	0005640	cellular_component	nuclear outer membrane
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0005886	cellular_component	plasma membrane
D	0005938	cellular_component	cell cortex
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0009615	biological_process	response to virus
D	0009986	cellular_component	cell surface
D	0010756	biological_process	positive regulation of plasminogen activation
D	0016020	cellular_component	membrane
D	0016829	molecular_function	lyase activity
D	0030308	biological_process	negative regulation of cell growth
D	0031430	cellular_component	M band
D	0042803	molecular_function	protein homodimerization activity
D	0045296	molecular_function	cadherin binding
D	0045892	biological_process	negative regulation of DNA-templated transcription
D	0045933	biological_process	positive regulation of muscle contraction
D	0046872	molecular_function	metal ion binding
D	0051020	molecular_function	GTPase binding
D	0061621	biological_process	canonical glycolysis
D	0070062	cellular_component	extracellular exosome
D	1903298	biological_process	negative regulation of hypoxia-induced intrinsic apoptotic signaling pathway
D	2001171	biological_process	positive regulation of ATP biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG A 701

Chain	Residue
A	GLN165
A	ASP244
A	GLU292
A	ASP317
A	LYS342
A	HOH712
A	HOH889

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 702

Chain	Residue
A	LYS342
A	HOH710
A	HOH711
A	SER39
A	ASP317

site_id	AC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG B 703

Chain	Residue
B	GLN165
B	ASP244
B	GLU292
B	ASP317
B	LYS342
B	HOH711
B	HOH712

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 704

Chain	Residue
B	SER39
B	ASP317
B	LYS342
B	HOH713
B	HOH718

site_id	AC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG C 705

Chain	Residue
C	GLN165
C	ASP244
C	GLU292
C	ASP317
C	LYS342
C	HOH712
C	HOH831

site_id	AC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 706

Chain	Residue
C	SER39
C	ASP317
C	LYS342
C	HOH732

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG D 707

Chain	Residue
D	GLN165
D	ASP244
D	GLU292
D	ASP317
D	LYS342
D	HOH721
D	HOH800

site_id	AC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 708

Chain	Residue
D	SER39
D	ASP317
D	LYS342
D	HOH757
D	HOH801

site_id	AC9
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 A 709

Chain	Residue
A	GLY37
A	ALA38
A	SER39
A	HIS157
A	GLN165
A	LYS342
A	ARG371
A	SER372
A	HOH711
A	HOH736

site_id	BC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PO4 B 710

Chain	Residue
B	GLY37
B	ALA38
B	SER39
B	HIS157
B	GLN165
B	LYS342
B	ARG371
B	SER372
B	HOH713
B	HOH722

site_id	BC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PO4 C 711

Chain	Residue
C	GLY37
C	ALA38
C	SER39
C	HIS157
C	GLN165
C	LYS342
C	ARG371
C	SER372

site_id	BC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PO4 D 712

Chain	Residue
D	GLY37
D	ALA38
D	SER39
D	HIS157
D	GLN165
D	LYS342
D	ARG371
D	SER372
D	HOH714

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	LEU339-SER352

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Region: {"description":"Epitope recognized by CAR and healthy patient antibodies"}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	28
Details	Region: {"description":"Epitope recognized by CAR antibodies"}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	560
Details	Region: {"description":"Required for repression of c-myc promoter activity"}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	4
Details	Active site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P00924","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P00924","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18560153","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	32
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P00924","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	4
Details	Modified residue: {"description":"N-acetylserine","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAR-2009","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Lilla S.","Zebisch A.","Kolch W."]}},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	32
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	16
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17182","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	16
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17182","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17182","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	4
Details	Modified residue: {"description":"N6-malonyllysine; alternate","evidences":[{"source":"PubMed","id":"21908771","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	4
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"28112733","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI22
Number of Residues	29
Details	Region: {"description":"Required for interaction with PLG","evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	GLU209
A	GLU166
A	HIS370
A	LYS393

site_id	CSA10
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
B	LYS342
B	HIS189

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

Chain	Residue	Details
C	LYS342
C	HIS189

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

Chain	Residue	Details
D	LYS342
D	HIS189

site_id	CSA13
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	LYS342
A	VAL240

site_id	CSA14
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
B	LYS342
B	VAL240

site_id	CSA15
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	LYS342
C	VAL240

site_id	CSA16
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	LYS342
D	VAL240

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

Chain	Residue	Details
B	GLU209
B	GLU166
B	HIS370
B	LYS393

site_id	CSA3
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	GLU209
C	GLU166
C	HIS370
C	LYS393

site_id	CSA4
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	GLU209
D	GLU166
D	HIS370
D	LYS393

site_id	CSA5
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	LYS342
A	GLU209
A	GLU166
A	HIS370

site_id	CSA6
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
B	LYS342
B	GLU209
B	GLU166
B	HIS370

site_id	CSA7
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
C	LYS342
C	GLU209
C	GLU166
C	HIS370

site_id	CSA8
Number of Residues	4
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
D	LYS342
D	GLU209
D	GLU166
D	HIS370

site_id	CSA9
Number of Residues	2
Details	Annotated By Reference To The Literature 1els

Chain	Residue	Details
A	LYS342
A	HIS189

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