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4ZA0

Structure of Human Enolase 2 in complex with Phosphonoacetohydroxamate

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
A0006094biological_processgluconeogenesis
A0006096biological_processglycolytic process
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0043025cellular_componentneuronal cell body
A0043204cellular_componentperikaryon
A0046872molecular_functionmetal ion binding
A0061621biological_processcanonical glycolysis
A0070062cellular_componentextracellular exosome
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
B0006094biological_processgluconeogenesis
B0006096biological_processglycolytic process
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0043025cellular_componentneuronal cell body
B0043204cellular_componentperikaryon
B0046872molecular_functionmetal ion binding
B0061621biological_processcanonical glycolysis
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue MG A 501
ChainResidue
AASP245
AGLU293
AASP318
APAH503
AHOH635

site_idAC2
Number of Residues4
Detailsbinding site for residue MG A 502
ChainResidue
ASER40
APAH503
AHOH633
AHOH702

site_idAC3
Number of Residues19
Detailsbinding site for residue PAH A 503
ChainResidue
AGLY38
AALA39
ASER40
AGLN166
AGLU167
AASP245
AGLU293
AASP318
ALEU341
ALYS343
AARG372
ASER373
ALYS394
AMG501
AMG502
AHOH633
AHOH641
AHOH702
AHOH706

site_idAC4
Number of Residues5
Detailsbinding site for residue MG B 501
ChainResidue
BASP245
BGLU293
BASP318
BPAH503
BHOH608

site_idAC5
Number of Residues4
Detailsbinding site for residue MG B 502
ChainResidue
BSER40
BPAH503
BHOH630
BHOH695

site_idAC6
Number of Residues19
Detailsbinding site for residue PAH B 503
ChainResidue
BGLY38
BALA39
BSER40
BGLN166
BGLU167
BASP245
BGLU293
BASP318
BLEU341
BLYS343
BARG372
BSER373
BLYS394
BMG501
BMG502
BHOH630
BHOH670
BHOH695
BHOH790

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
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P00924
ChainResidueDetails
AGLU210
BGLU210

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00924
ChainResidueDetails
ALYS343
BLYS343

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ASER40
BSER40

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00924
ChainResidueDetails
AHIS158
BASP318
BSER370
BLYS394
AGLU167
AGLU293
AASP318
ASER370
ALYS394
BHIS158
BGLU167
BGLU293

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP245
BASP245

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ALYS5
ALYS64
ALYS193
ALYS256
BLYS5
BLYS64
BLYS193
BLYS256

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ATHR26
BTHR26

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR44
BTYR44

site_idSWS_FT_FI10
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
ChainResidueDetails
ALYS60
ALYS89
ALYS228
BLYS60
BLYS89
BLYS228

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17183
ChainResidueDetails
ALYS197
ALYS199
BLYS197
BLYS199

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182
ChainResidueDetails
ALYS202
BLYS202

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ALYS233
BLYS233

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER263
BSER263

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ATYR287
BTYR287

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ASER291
BSER291

site_idSWS_FT_FI17
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17182
ChainResidueDetails
ALYS335
ALYS343
ALYS406
BLYS335
BLYS343
BLYS406

site_idSWS_FT_FI18
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ALYS202
BLYS202

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PDB entries from 2024-12-25

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