1E50: AML1/CBFbeta complex

Name: PDB 1E50: AML1/CBFbeta complex
Published: 2001-07-12
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transcription

AML1/CBFbeta complex. Determined by X-ray diffraction at 2.6 Å resolution. Released 12 Jul 2001.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: HOMO SAPIENS
Chains: 10
Atoms: 9,696
Mol. weight: 152.72 kDa
Released: 12 Jul 2001

Explore 1E50 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1E50 contains 27 α-helices and 113 β-strands across 10 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: 2 helices, 14 β-strands

Element	Residues	Length	Sheet
β-strand	60-64	5	1
β-strand	70-73	4	1
α-helix	74-76	3
β-strand	78-80	3	2
α-helix	83-85	3
β-strand	90-93	4	1
β-strand	102-108	7	3
β-strand	115	1	3
β-strand	117-118	2	4
β-strand	121-123	3	3
β-strand	124	1	1
β-strand	128-130	3	1
β-strand	135-136	2	4
β-strand	146-152	7	3
β-strand	158-166	9	3
β-strand	167-169	3	2

Chain B: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	8-14	7
α-helix	16-19	4
β-strand	25-29	5	3
α-helix	37-49	13
β-strand	52-54	3	5
β-strand	55-57	3	3
β-strand	62	1	3
β-strand	65-67	3	5
α-helix	80-82	3
β-strand	86-87	2	3
β-strand	94-103	10	3
β-strand	106-115	10	3
β-strand	120-127	8	3
α-helix	129-134	6

Chains C, E and G: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	60-64	5	1
β-strand	70-73	4	1
β-strand	78-80	3	6
α-helix	83-85	3
β-strand	90-93	4	1
β-strand	102-108	7	7
β-strand	117-118	2	8
β-strand	121-123	3	7
β-strand	124-125	2	1
β-strand	128-130	3	1
β-strand	135-136	2	8
α-helix	144-145	2
β-strand	146-152	7	7
β-strand	158-166	9	7
β-strand	167-169	3	6

Chain D: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	8-14	7
α-helix	16-22	7
β-strand	25-29	5	7
α-helix	37-49	13
β-strand	52-57	6	7
β-strand	62-67	6	7
β-strand	86-91	6	7
β-strand	94-103	10	7
β-strand	106-115	10	7
β-strand	120-127	8	7
α-helix	129-133	5

Chain F: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	8-14	7
α-helix	16-22	7
β-strand	25-29	5	11
α-helix	37-49	13
β-strand	52-57	6	11
β-strand	62-67	6	11
β-strand	86-87	2	11
β-strand	94-103	10	11
β-strand	106-115	10	11
β-strand	120-127	8	11
α-helix	129-133	5

Chain H: 4 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	8-14	7
α-helix	16-22	7
β-strand	25-29	5	14
α-helix	37-49	13
β-strand	52-54	3	16
β-strand	55-57	3	14
β-strand	62	1	14
β-strand	65-67	3	16
β-strand	86-87	2	14
β-strand	94-103	10	14
β-strand	106-115	10	14
β-strand	120-127	8	14
α-helix	129-133	5

Chain Q: 1 helix, 15 β-strands

Element	Residues	Length	Sheet
β-strand	63-64	2	17
β-strand	70-72	3	17
β-strand	78-80	3	18
β-strand	90-93	4	17
β-strand	102-104	3	19
β-strand	107	1	20
β-strand	115	1	20
β-strand	117-118	2	21
β-strand	121-123	3	19
β-strand	125	1	17
β-strand	128-130	3	17
β-strand	135-136	2	21
α-helix	144-145	2
β-strand	146-152	7	19
β-strand	158-166	9	19
β-strand	167-169	3	18

Chain R: 1 helix, 13 β-strands

Element	Residues	Length	Sheet
β-strand	63-64	2	22
β-strand	70-72	3	22
β-strand	78-80	3	23
β-strand	89-93	5	22
β-strand	102-104	3	24
β-strand	117-118	2	25
β-strand	121-123	3	24
β-strand	125	1	22
β-strand	128-131	4	22
β-strand	135-136	2	25
α-helix	144-145	2
β-strand	146-152	7	26
β-strand	158-166	9	26
β-strand	167-169	3	23

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Core-binding factor alpha subunit	A, C, E, G, Q, R	protein	134	HOMO SAPIENS	Q01196 (AlphaFold model)
Core-binding factor cbf-beta	B, D, F, H	protein	134	HOMO SAPIENS	Q13951 (AlphaFold model)

Sequence of entity 1 (A, C, E, G, Q, R), FASTA

>1E50_1 CORE-BINDING FACTOR ALPHA SUBUNIT (chains A, C, E, G, Q, R)
SMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGN
DENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKIT
VDGPREPRRHRQKL

Sequence of entity 2 (B, D, F, H), FASTA

>1E50_2 CORE-BINDING FACTOR CBF-BETA (chains B, D, F, H)
PRVVPDQRSKFENEEFFRKLSRECEIKYTGFRDRPHEERQARFQNACRDGRSEIAFVATG
TNLSLQFFPASWQGEQRQTPSREYVDLEREAGKVYLKAPMILNGVCVIWKGWIDLQRLDG
MGCLEFDEERAQQE

Primary citation

Structural Basis for the Heterodimeric Interaction between the Acute Leukaemia-Associated Transcription Factors Aml1 and Cbfbeta. Warren, A.J., Bravo, J., Williams, R.L. et al. EMBO J (2000) 19:3004. DOI 10.1093/EMBOJ/19.12.3004 · PubMed

Other PDB entries of the same protein (UniProt Q01196 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1LJM 2.5 Å, DNA recognition is mediated by conformational transition and by DNA bending
1H9D 2.6 Å, Aml1/cbf-beta/dna complex
1CMO Immunoglobulin motif DNA-recognition and heterodimerization for the PEBP2/CBF runt-domain
1CO1 Fold of the cbfa

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