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4ZCW

Structure of Human Enolase 2 in complex with SF2312

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0001917cellular_componentphotoreceptor inner segment
A0004634molecular_functionphosphopyruvate hydratase activity
A0005515molecular_functionprotein binding
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0005938cellular_componentcell cortex
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0009410biological_processresponse to xenobiotic stimulus
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0019899molecular_functionenzyme binding
A0030426cellular_componentgrowth cone
A0032355biological_processresponse to estradiol
A0042802molecular_functionidentical protein binding
A0043025cellular_componentneuronal cell body
A0043204cellular_componentperikaryon
A0044877molecular_functionprotein-containing complex binding
A0045121cellular_componentmembrane raft
A0046872molecular_functionmetal ion binding
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
A0097060cellular_componentsynaptic membrane
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0001917cellular_componentphotoreceptor inner segment
B0004634molecular_functionphosphopyruvate hydratase activity
B0005515molecular_functionprotein binding
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0005938cellular_componentcell cortex
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0009410biological_processresponse to xenobiotic stimulus
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0019899molecular_functionenzyme binding
B0030426cellular_componentgrowth cone
B0032355biological_processresponse to estradiol
B0042802molecular_functionidentical protein binding
B0043025cellular_componentneuronal cell body
B0043204cellular_componentperikaryon
B0044877molecular_functionprotein-containing complex binding
B0045121cellular_componentmembrane raft
B0046872molecular_functionmetal ion binding
B0061621biological_processcanonical glycolysis
B0070062cellular_componentextracellular exosome
B0097060cellular_componentsynaptic membrane
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue 4NG A 501
ChainResidue
AGLY38
ALEU341
ALYS343
AHIS371
AARG372
ASER373
ALYS394
AMG502
AMG503
AHOH642
AHOH681
AALA39
ASER40
AGLN166
AGLU167
AGLU210
AASP245
AGLU293
AASP318

site_idAC2
Number of Residues5
Detailsbinding site for residue MG A 502
ChainResidue
AASP245
AGLU293
AASP318
A4NG501
AHOH619

site_idAC3
Number of Residues4
Detailsbinding site for residue MG A 503
ChainResidue
ASER40
A4NG501
AHOH642
AHOH681

site_idAC4
Number of Residues19
Detailsbinding site for residue 4NG B 501
ChainResidue
BGLY38
BALA39
BSER40
BGLN166
BGLU167
BGLU210
BASP245
BGLU293
BASP318
BLEU341
BLYS343
BHIS371
BARG372
BSER373
BLYS394
BMG502
BMG503
BHOH676
BHOH703

site_idAC5
Number of Residues4
Detailsbinding site for residue MG B 502
ChainResidue
BSER40
B4NG501
BHOH676
BHOH703

site_idAC6
Number of Residues6
Detailsbinding site for residue MG B 503
ChainResidue
BASP245
BGLU293
BASP318
BLYS394
B4NG501
BHOH639

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLLKvNQIGSVTEA
ChainResidueDetails
ALEU340-ALA353

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"UniProtKB","id":"P00924","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"P00924","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P00924","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N-acetylserine","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"15592455","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17182","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17183","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17182","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P17182","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P06733","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

239492

PDB entries from 2025-07-30

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