9X4F: Alpha-enolase

Crystal structure of tetrameric alpha-enolase with asymmetric flexible active sites. Determined by X-ray diffraction at 2.7 Å resolution. Released 15 Jul 2026.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 13,656
Mol. weight: 195.4 kDa
Ligands: MG
Released: 15 Jul 2026

Explore 9X4F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9X4F contains 99 α-helices and 78 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: 26 helices, 21 β-strands

Element	Residues	Length	Sheet
α-helix	-7--4	4
β-strand	3	1	1
β-strand	5-12	8	2
β-strand	18-26	9	2
β-strand	29-34	6	2
α-helix	46-49	4
α-helix	57-59	3
α-helix	63-67	5
α-helix	68-73	6
α-helix	74-77	4
β-strand	78	1	1
α-helix	87-98	12
α-helix	108-126	19
α-helix	130-138	9
β-strand	145	1	3
α-helix	146	1
β-strand	147-148	2	4
β-strand	150-154	5	4
α-helix	156-158	3
β-strand	167-171	5	4
α-helix	178-200	23
α-helix	202-205	4
β-strand	207	1	4
β-strand	213	1	4
α-helix	220-234	15
β-strand	241-245	5	4
α-helix	248-250	3
β-strand	252-253	2	5
β-strand	256-257	2	5
α-helix	264-265	2
α-helix	267-269	3
β-strand	271	1	5
α-helix	273-286	14
β-strand	289-293	5	4
α-helix	301-310	10
β-strand	314-317	4	4
α-helix	325-334	10
β-strand	339-342	4	4
α-helix	344-347	4
α-helix	350-362	13
β-strand	366-370	5	4
α-helix	380-388	9
β-strand	392-394	3	4
α-helix	401-417	17
α-helix	418-420	3
β-strand	423	1	3
α-helix	425-427	3

Chain B: 24 helices, 18 β-strands

Element	Residues	Length	Sheet
β-strand	5-12	8	6
β-strand	18-26	9	6
β-strand	29-34	6	6
α-helix	35-37	3
α-helix	46-49	4
α-helix	57-59	3
α-helix	63-67	5
α-helix	68-73	6
α-helix	74-79	6
α-helix	87-98	12
α-helix	108-125	18
α-helix	130-137	8
β-strand	145	1	7
α-helix	146	1
β-strand	147-154	8	4
β-strand	167-171	5	4
α-helix	178-200	23
α-helix	202-205	4
β-strand	207	1	4
β-strand	213	1	4
α-helix	220-234	15
β-strand	241-245	5	4
α-helix	248-250	3
β-strand	252-253	2	8
β-strand	256-257	2	8
α-helix	267-269	3
β-strand	271	1	8
α-helix	273-286	14
β-strand	289-293	5	4
α-helix	301-310	10
β-strand	314-317	4	4
α-helix	325-334	10
β-strand	339-342	4	4
α-helix	344-347	4
α-helix	350-362	13
β-strand	366-370	5	4
α-helix	380-388	9
β-strand	392-394	3	4
α-helix	401-417	17
α-helix	418-420	3
β-strand	423	1	7
α-helix	425-427	3

Chain C: 24 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	5-12	8	9
β-strand	18-26	9	9
β-strand	29-34	6	9
β-strand	37	1	10
α-helix	46-47	2
α-helix	57-59	3
α-helix	63-67	5
α-helix	68-73	6
α-helix	74-80	7
α-helix	87-98	12
α-helix	108-126	19
α-helix	130-137	8
β-strand	145	1	11
α-helix	146	1
β-strand	147-154	8	12
α-helix	156-158	3
β-strand	167-171	5	12
α-helix	178-200	23
α-helix	202-205	4
β-strand	207	1	12
β-strand	213	1	12
α-helix	220-234	15
β-strand	241-245	5	12
β-strand	252-253	2	13
β-strand	256-257	2	13
α-helix	265	1
α-helix	267-269	3
β-strand	271	1	13
α-helix	273-286	14
β-strand	289-293	5	12
α-helix	301-311	11
β-strand	314-317	4	12
α-helix	325-333	9
β-strand	339-342	4	12
α-helix	344-347	4
α-helix	350-362	13
β-strand	366-370	5	12
β-strand	374	1	10
α-helix	380-387	8
β-strand	391-394	4	12
α-helix	401-417	17
α-helix	418-420	3
β-strand	423	1	11
α-helix	425-427	3

Chain D: 25 helices, 19 β-strands

Element	Residues	Length	Sheet
β-strand	5-12	8	14
β-strand	18-26	9	14
β-strand	29-34	6	14
α-helix	46-49	4
α-helix	57-59	3
α-helix	63-68	6
α-helix	69-73	5
α-helix	74-80	7
α-helix	87-98	12
α-helix	108-126	19
α-helix	130-138	9
β-strand	145	1	15
α-helix	146	1
β-strand	147-148	2	16
β-strand	150-154	5	16
α-helix	156-158	3
β-strand	167-171	5	16
α-helix	178-200	23
α-helix	202-205	4
β-strand	207	1	12
β-strand	213	1	16
α-helix	220-234	15
β-strand	241-245	5	16
α-helix	248-251	4
β-strand	252-253	2	17
β-strand	256-257	2	17
α-helix	265	1
α-helix	267-269	3
β-strand	271	1	17
α-helix	273-286	14
β-strand	289-293	5	16
α-helix	301-310	10
β-strand	314-317	4	16
α-helix	325-333	9
β-strand	339-342	4	16
α-helix	344-347	4
α-helix	350-362	13
β-strand	366-370	5	16
α-helix	380-388	9
β-strand	392-394	3	16
α-helix	401-417	17
α-helix	418-420	3
β-strand	423	1	15
α-helix	425-427	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Alpha-enolase	A, B, C, D	protein	447	Homo sapiens	P06733 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>9X4F_1 Alpha-enolase (chains A, B, C, D)
MHHHHHHLVPRGSMSILKIHAREIFDSRGNPTVEVDLFTSKGLFRAAVPSGASTGIYEAL
ELRDNDKTRYMGKGVSKAVEHINKTIAPALVSKKLNVTEQEKIDKLMIEMDGTENKSKFG
ANAILGVSLAVCKAGAVEKGVPLYRHIADLAGNSEVILPVPAFNVINGGSHAGNKLAMQE
FMILPVGAANFREAMRIGAEVYHNLKNVIKEKYGKDATNVGDEGGFAPNILENKEGLELL
KTAIGKAGYTDKVVIGMDVAASEFFRSGKYDLDFKSPDDPSRYISPDQLADLYKSFIKDY
PVVSIEDPFDQDDWGAWQKFTASAGIQVVGDDLTVTNPKRIAKAVNEKSCNCLLLKVNQI
GSVTESLQACKLAQANGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKY
NQLLRIEEELGSKAKFAGRNFRNPLAK

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	8

Primary citation

Natural Glycoside OSW-1 Targets Glycolytic Enzyme Enolase 1 to Reprogram Tumor Metabolism via Glycolytic Blockade. Xia, Y., Xia, M., Dai, Z. et al. ACS Chem Biol (2026) 21:790-800. DOI 10.1021/acschembio.6c00022 · PubMed

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

5NI9 1.33 Å, Crystal structure of HLA-DRB1*04:01 with the alpha-enolase peptide 326-340
5NIG 1.35 Å, Crystal structure of HLA-DRB1*04:01 with modified alpha-enolase peptide 326-340…
5OCK 1.6 Å, Crystal structure of ACPA E4 in complex with CEP1
5JLZ 1.99 Å, Crystal structure of HLA-DRB1*04:01 in complex with modified alpha-enolase peptide 26-40…
2PSN 2.2 Å, Crystal structure of enolase1
3B97 2.2 Å, Crystal Structure of human Enolase 1
8TRL 2.4 Å, T cell recognition of citrullinated alpha-enolase peptide presented by HLA-DR4
5LAX 2.6 Å, Crystal structure of HLA_DRB1*04:01 in complex with alpha-enolase peptide 26-40
9A0U Docking model of HLA class I with HLA class II

Browse structure collections

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