Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

3H8A

Crystal structure of E. coli enolase bound to its cognate RNase E recognition domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0000015cellular_componentphosphopyruvate hydratase complex
A0000287molecular_functionmagnesium ion binding
A0004634molecular_functionphosphopyruvate hydratase activity
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0005856cellular_componentcytoskeleton
A0006096biological_processglycolytic process
A0006396biological_processRNA processing
A0006401biological_processRNA catabolic process
A0009986cellular_componentcell surface
A0016020cellular_componentmembrane
A0016829molecular_functionlyase activity
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046872molecular_functionmetal ion binding
A1990061cellular_componentbacterial degradosome
B0000015cellular_componentphosphopyruvate hydratase complex
B0000287molecular_functionmagnesium ion binding
B0004634molecular_functionphosphopyruvate hydratase activity
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005856cellular_componentcytoskeleton
B0006096biological_processglycolytic process
B0006396biological_processRNA processing
B0006401biological_processRNA catabolic process
B0009986cellular_componentcell surface
B0016020cellular_componentmembrane
B0016829molecular_functionlyase activity
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046872molecular_functionmetal ion binding
B1990061cellular_componentbacterial degradosome
C0000015cellular_componentphosphopyruvate hydratase complex
C0000287molecular_functionmagnesium ion binding
C0004634molecular_functionphosphopyruvate hydratase activity
C0005515molecular_functionprotein binding
C0005576cellular_componentextracellular region
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0005856cellular_componentcytoskeleton
C0006096biological_processglycolytic process
C0006396biological_processRNA processing
C0006401biological_processRNA catabolic process
C0009986cellular_componentcell surface
C0016020cellular_componentmembrane
C0016829molecular_functionlyase activity
C0042802molecular_functionidentical protein binding
C0042803molecular_functionprotein homodimerization activity
C0046872molecular_functionmetal ion binding
C1990061cellular_componentbacterial degradosome
D0000015cellular_componentphosphopyruvate hydratase complex
D0000287molecular_functionmagnesium ion binding
D0004634molecular_functionphosphopyruvate hydratase activity
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005737cellular_componentcytoplasm
D0005829cellular_componentcytosol
D0005856cellular_componentcytoskeleton
D0006096biological_processglycolytic process
D0006396biological_processRNA processing
D0006401biological_processRNA catabolic process
D0009986cellular_componentcell surface
D0016020cellular_componentmembrane
D0016829molecular_functionlyase activity
D0042802molecular_functionidentical protein binding
D0042803molecular_functionprotein homodimerization activity
D0046872molecular_functionmetal ion binding
D1990061cellular_componentbacterial degradosome
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG A 1431
ChainResidue
AASP245
AGLU289
AASP316
AHOH512
AHOH878
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG C 1431
ChainResidue
CASP245
CGLU289
CASP316
CHOH879
Functional Information from PROSITE/UniProt
site_idPS00164
Number of Residues14
DetailsENOLASE Enolase signature. ILIKfNQIGSLTET
ChainResidueDetails
AILE338-THR351
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues116
DetailsRegion: {"description":"Interaction with RNase E"}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15003462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"15003462","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30714720","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11676541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16516921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H8A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11676541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30714720","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3H8A","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11676541","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16516921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1E9I","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2FYM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00318","evidenceCode":"ECO:0000255"},{"source":"PDB","id":"6BFY","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6BFZ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues12
DetailsSite: {"description":"Interaction with RNase E","evidences":[{"source":"PubMed","id":"16516921","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20823555","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"18723842","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"N6-(2-hydroxyisobutyryl)lysine","evidences":[{"source":"PubMed","id":"31328167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues17
DetailsRegion: {"description":"Interaction with enolase"}
ChainResidueDetails

240971

PDB entries from 2025-08-27

PDB statisticsPDBj update infoContact PDBjnumon