3B97: Human Enolase 1

Crystal Structure of human Enolase 1. Determined by X-ray diffraction at 2.2 Å resolution. Released 16 Sept 2008.

Method
X-ray diffraction
Resolution
2.2 Å
Organism
Homo sapiens
Chains
4
Atoms
13,815
Mol. weight
188.97 kDa
Ligands
MG
Released
16 Sept 2008

Explore 3B97 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3B97 contains 95 α-helices and 81 β-strands across 4 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 24 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand4-1181
β-strand17-2591
β-strand28-3361
β-strand3612
α-helix45-462
α-helix56-583
α-helix62-665
α-helix67-726
α-helix73-786
α-helix86-9712
α-helix107-12418
α-helix129-1379
β-strand14413
α-helix1451
β-strand146-15384
α-helix155-1573
β-strand166-17054
α-helix177-19923
α-helix201-2033
β-strand20614
β-strand21214
α-helix219-23214
β-strand240-24454
α-helix247-2493
β-strand251-25335
β-strand255-25625
α-helix266-2683
β-strand27015
α-helix272-28514
β-strand288-29254
α-helix300-31011
β-strand313-31644
α-helix324-33310
β-strand338-34144
α-helix343-3464
α-helix349-36113
β-strand365-36954
β-strand37312
α-helix379-3868
β-strand391-39334
α-helix400-41617
α-helix417-4193
β-strand42213
α-helix424-4263
Chain B: 24 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand4-1186
β-strand17-2596
β-strand28-3366
β-strand3617
α-helix45-462
α-helix56-583
α-helix62-676
α-helix68-725
α-helix73-797
α-helix86-9712
α-helix107-12519
α-helix129-1379
β-strand14418
α-helix1451
β-strand146-15384
α-helix155-1573
β-strand166-17054
α-helix177-19923
α-helix201-2033
β-strand20614
β-strand21214
α-helix219-23214
β-strand240-24454
α-helix247-2504
β-strand251-25229
β-strand255-25629
α-helix266-2683
β-strand27019
α-helix272-28514
β-strand288-29254
α-helix300-31011
β-strand313-31644
α-helix324-33310
β-strand338-34144
α-helix343-3464
α-helix349-36113
β-strand365-36954
β-strand37317
α-helix379-3868
β-strand391-39334
α-helix400-41617
α-helix417-4193
β-strand42218
α-helix424-4263
Chain C: 24 helices, 21 β-strands
ElementResiduesLengthSheet
β-strand4-11810
β-strand17-25910
β-strand28-33610
β-strand36111
α-helix45-462
α-helix56-583
α-helix62-665
α-helix67-726
α-helix73-797
α-helix86-9712
α-helix107-12418
α-helix129-1379
β-strand144112
α-helix1451
β-strand146-147213
β-strand149-153513
α-helix155-1573
β-strand166-170513
α-helix177-19923
α-helix201-2033
β-strand206113
β-strand212113
α-helix219-23315
β-strand240-244513
α-helix247-2504
β-strand251-252214
β-strand255-256214
α-helix266-2683
β-strand270114
α-helix272-28514
β-strand288-292513
α-helix300-31011
β-strand313-316413
α-helix324-33310
β-strand338-341413
α-helix343-3464
α-helix349-36113
β-strand365-369513
β-strand373111
α-helix379-3879
β-strand391-393313
α-helix400-41617
α-helix417-4193
β-strand422112
α-helix424-4263
Chain D: 23 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand4-11815
β-strand17-25915
β-strand28-33615
β-strand36116
α-helix45-462
α-helix56-583
α-helix62-665
α-helix67-726
α-helix73-797
α-helix86-9712
α-helix107-12418
α-helix129-1379
β-strand144117
α-helix1451
β-strand146-153813
α-helix155-1573
β-strand166-170513
α-helix177-19923
α-helix201-2033
β-strand206113
β-strand212113
α-helix219-23315
β-strand240-244513
α-helix247-2504
β-strand251-252218
β-strand255-256218
β-strand270118
α-helix272-28514
β-strand288-292513
α-helix300-31011
β-strand313-316413
α-helix324-3329
β-strand338-341413
α-helix343-3464
α-helix349-36113
β-strand365-369513
β-strand373116
α-helix379-3879
β-strand391-393313
α-helix400-41617
α-helix417-4193
β-strand422117
α-helix424-4263

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Alpha-enolaseA, B, C, Dprotein433Homo sapiensP06733 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>3B97_1 Alpha-enolase (chains A, B, C, D)
SILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEALELRDNDKTRYMGKG
VSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFGANAILGVSLAVCKA
GAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQEFMILPVGAANFREA
MRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELLKTAIGKAGYTDKVV
IGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDYPVVSIEDPFDQDDW
GAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQIGSVTESLQACKLAQ
ANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLLRIEEELGSKA
KFAGRNFRNPLAK

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg8

Water and common crystallization additives (SO4) are not listed.

Primary citation

Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme. Kang, H.J., Jung, S.K., Kim, S.J. et al. Acta Crystallogr D Biol Crystallogr (2008) 64:651-657. DOI 10.1107/S0907444908008561 · PubMed

Other PDB entries of the same protein (UniProt P06733 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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