9EL5: FANCM translocase domain

FANCM translocase domain bound to DNA. Determined by X-ray diffraction at 2.2 Å resolution. Released 18 Jun 2025.

Method: X-ray diffraction
Resolution: 2.2 Å
Organisms: Homo sapiens, synthetic construct
Chains: 2
Atoms: 5,186
Mol. weight: 78.55 kDa
Released: 18 Jun 2025

Explore 9EL5 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9EL5 contains 28 α-helices and 15 β-strands across 1 chain. 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: 28 helices, 15 β-strands

Element	Residues	Length	Sheet
α-helix	77-80	4
β-strand	82-86	5	1
α-helix	93-104	12
β-strand	107-110	4	2
α-helix	117-131	15
β-strand	136-140	5	2
α-helix	144-157	14
α-helix	162-164	3
β-strand	165-168	4	2
α-helix	174-183	10
β-strand	186-189	4	2
α-helix	191-199	9
α-helix	205-207	3
β-strand	208-214	7	2
α-helix	216-218	3
α-helix	224-232	9
β-strand	240-244	5	2
α-helix	252-261	10
β-strand	266-269	4	2
α-helix	275-278	4
α-helix	285	1
β-strand	286-291	6	3
α-helix	295-318	24
α-helix	326-328	3
α-helix	331-341	11
α-helix	352-376	25
α-helix	379-390	12
α-helix	398-404	7
α-helix	407-419	13
α-helix	448-466	19
α-helix	475-477	3
β-strand	479-482	4	3
α-helix	486-497	12
β-strand	505-508	4	3
α-helix	522-533	12
β-strand	539-542	4	3
α-helix	544-546	3
β-strand	557-560	4	3
α-helix	568-574	7
β-strand	584-590	7	3
α-helix	593-613	21
α-helix	635	1
β-strand	636-640	5	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fanconi anemia group M protein	A	protein	573	Homo sapiens	Q8IYD8 (AlphaFold model)
DNA (37-mer)	P	DNA	43	synthetic construct

Sequence of entity 1 (A), FASTA

>9EL5_1 Fanconi anemia group M protein (chains A)
GGGFCTSAGALWIYPTNCPVRDYQLHISRAALFCNTLVCLPTGLGKTFIAAVVMYNFYRW
FPSGKVVFMAPTKPLVTQQIEACYQVMGIPQSHMAEMTGSTQASTRKEIWCSKRVLFLTP
QVMVNDLSRGACPAAEIKCLVIDEAHKALGNYAYCQVVRELVKYTNHFRILALSATPGSD
IKAVQQVITNLLIGQIELRSEDSPDILTYSHERKVEKLIVPLGEELAAIQKTYIQILESF
ARSLIQRNVLMRRDIPNLTKYQIILARDQFRKNPSPNIVGIQQGIIEGEFAICISLYHGY
ELLQQMGMRSLYFFLCGIMDGTKGMTRSKNELGRNEDFMKLYNHLECMFARTRSTSANGI
SAIQQGDKNKKFVYSHPKLKKLEEVVIEHFKSWNAENTTEKKRDETRVMIFSSFRDSVQE
IAEMLSQHQPIIRVMTFVGHASGKSTKGFTQKEQLEVVKQFRDGGYNTLVSTCVGEEGLD
IGEVDLIICFDSQKSPIRLVQRMGRTGRKRQGRIVIILSEGREERIYNQSQSNKRSIYKA
ISSNRQVLHFYQRSPRMVPDGINPKLHKMFITH

Sequence of entity 2 (P), FASTA

>9EL5_2 DNA (37-MER) (chains P)
GGTATGAGCACTGCTTAGGCAGTGCTCATACCGCATGGAGCTG

Primary citation

Structural basis of Fanconi anemia pathway activation by FANCM. Bythell-Douglas, R., van Twest, S., Abbouche, L. et al. EMBO J (2025) 44:4013-4036. DOI 10.1038/s44318-025-00468-3 · PubMed

Other PDB entries of the same protein (UniProt Q8IYD8 (AlphaFold model), which also has an AlphaFold model), best resolution first:

4E45 2.0 Å, Crystal structure of the hMHF1/hMHF2 Histone-Fold Tetramer in Complex with Fanconi…
4BXO 2.15 Å, Architecture and DNA recognition elements of the Fanconi anemia FANCM- FAAP24 complex
9HJO 2.4 Å, FANCM-FAAP24-dsDNA complex
4DRB 2.63 Å, The crystal structure of FANCM bound MHF complex
4M6W 2.9 Å, Crystal structure of the C-terminal segment of FANCM in complex with FAAP24
4DAY 3.3 Å, Crystal structure of the RMI core complex with MM2 peptide from FANCM

Browse structure collections

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