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3UJS

Asymmetric complex of human neuron specific enolase-6-PGA/PEP

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 600
ChainResidue
AASP244
AGLU292
AASP317
AXSP602
AHOH719

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 601
ChainResidue
ASER39
AXSP602
AHOH849
AHOH851

site_idAC3
Number of Residues19
DetailsBINDING SITE FOR RESIDUE XSP A 602
ChainResidue
AGLY37
AALA38
ASER39
AHIS157
AGLN165
AGLU166
AGLU209
AASP244
AGLU292
AASP317
ALYS342
AHIS370
AARG371
ASER372
ALYS393
AMG600
AMG601
AHOH849
AHOH851

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE TRS A 603
ChainResidue
ATHR40
AILE42
AGLU249
AGLN297
AHOH763
AHOH775
AHOH1012
AHOH1041

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 600
ChainResidue
BASP244
BGLU292
BASP317
B0V5602
BHOH961

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 601
ChainResidue
BSER39
B0V5602
BHOH887
BHOH888

site_idAC7
Number of Residues19
DetailsBINDING SITE FOR RESIDUE 0V5 B 602
ChainResidue
BGLY37
BALA38
BSER39
BGLN165
BGLU166
BGLU209
BASP244
BGLU292
BASP317
BLYS342
BHIS370
BARG371
BSER372
BLYS393
BMG600
BMG601
BHOH887
BHOH888
BHOH1022

Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. LLLKvNQIGSVTEA
ChainResidueDetails
ALEU339-ALA352

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:P00924
ChainResidueDetails
AGLU209
BGLU209

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P00924
ChainResidueDetails
ALYS342
BLYS342

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ASER39
BSER39

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P00924
ChainResidueDetails
AHIS157
BASP317
BSER369
BLYS393
AGLU166
AGLU292
AASP317
ASER369
ALYS393
BHIS157
BGLU166
BGLU292

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AASP244
BASP244

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ASER1
BSER1

site_idSWS_FT_FI7
Number of Residues8
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ALYS4
ALYS63
ALYS192
ALYS255
BLYS4
BLYS63
BLYS192
BLYS255

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:20068231
ChainResidueDetails
ATHR25
BTHR25

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455
ChainResidueDetails
ATYR43
BTYR43

site_idSWS_FT_FI10
Number of Residues6
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P17182
ChainResidueDetails
ALYS59
ALYS88
ALYS227
BLYS59
BLYS88
BLYS227

site_idSWS_FT_FI11
Number of Residues4
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17183
ChainResidueDetails
ALYS196
ALYS198
BLYS196
BLYS198

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P17182
ChainResidueDetails
ALYS201
BLYS201

site_idSWS_FT_FI13
Number of Residues2
DetailsMOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ALYS232
BLYS232

site_idSWS_FT_FI14
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER262
BSER262

site_idSWS_FT_FI15
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ATYR286
BTYR286

site_idSWS_FT_FI16
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P06733
ChainResidueDetails
ASER290
BSER290

site_idSWS_FT_FI17
Number of Residues6
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P17182
ChainResidueDetails
ALYS334
ALYS342
ALYS405
BLYS334
BLYS342
BLYS405

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
ALYS201
BLYS201

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PDB entries from 2024-10-16

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