Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3UCC

Asymmetric complex of human neuron specific enolase-1-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
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 Residues5
DetailsBINDING SITE FOR RESIDUE MG A 599
ChainResidue
AASP244
AGLU292
AASP317
A2PG601
AHOH800

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 600
ChainResidue
ASER39
A2PG601
AHOH801
AHOH802

site_idAC3
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 2PG A 601
ChainResidue
AGLY37
AALA38
ASER39
AHIS157
AGLN165
AGLU166
AGLU209
AASP244
AGLU292
AASP317
ALYS342
AHIS370
AARG371
ASER372
ALYS393
AMG599
AMG600
AHOH800
AHOH801
AHOH802

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE TRS A 700
ChainResidue
ATHR40
ASER248
AGLU249
AGLN297
AHOH906

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG B 599
ChainResidue
BASP244
BGLU292
BASP317
B2PG601
BHOH800

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG B 600
ChainResidue
BSER39
B2PG601
BHOH801
BHOH802

site_idAC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE 2PG B 601
ChainResidue
BGLY37
BALA38
BSER39
BGLN165
BGLU166
BGLU209
BASP244
BGLU292
BASP317
BLEU340
BLYS342
BHIS370
BARG371
BSER372
BLYS393
BHOH475
BMG599
BMG600
BHOH801
BHOH802

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
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

238582

PDB entries from 2025-07-09

PDB statisticsPDBj update infoContact PDBjnumon